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All-atom empirical potential for molecular modeling and dynamics studies of proteins.
- All-atom empirical potential for molecular modeling and dynamics analysis of proteins.
Protein parameters are reported for the all-atom empirical vitality function inside the CHARMM program. The parameter evaluation was based on a self-consistent technique designed to appreciate a steadiness between the interior (bonding) and interaction (nonbonding) phrases of the facility space and among the many many solvent-solvent, solvent-solute, and solute-solute interactions.
Optimization of the inside parameters used experimental gas-phase geometries, vibrational spectra, and torsional vitality surfaces supplemented with ab initio outcomes.
The peptide backbone bonding parameters had been optimized with respect to data for N-methylacetamide and the alanine dipeptide.
The interaction parameters, considerably the atomic prices, had been determined by changing into ab initio interaction energies and geometries of complexes between water and model compounds that represented the backbone and the various facet chains.
In addition to, dipole moments, experimental heats and free energies of vaporization, solvation and sublimation, molecular volumes, and crystal pressures and constructions had been used inside the optimization.
The following protein parameters had been examined by making use of them to noncyclic tripeptide crystals, cyclic peptide crystals, and the proteins crambin, bovine pancreatic trypsin inhibitor, and carbonmonoxy myoglobin in vacuo and in crystals.
An in depth analysis of the connection between the alanine dipeptide potential vitality ground and calculated protein φ, χ angles was made and utilized in optimizing the peptide group torsional parameters.
The outcomes exhibit that use of ab initio structural and energetic data by themselves aren’t ample to accumulate an passable backbone illustration for peptides and proteins in decision and in crystals.
Intensive comparisons between molecular dynamics simulations and experimental data for polypeptides and proteins had been carried out for every structural and dynamic properties.
Vitality minimization and dynamics simulations for crystals exhibit that the latter are needed to accumulate vital comparisons with experimental crystal constructions.
The launched parameters, along with the beforehand printed CHARMM all-atom parameters for nucleic acids and lipids, current a relentless set for condensed-phase simulations of all types of molecules of natural curiosity.
Anti-Human VEGFR-1/Flt-1 (Peptide), soluble Antibody |
102-PA21 |
ReliaTech |
200 µg |
EUR 204.75 |
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. |
Anti-Human VEGFR-1/Flt-1 (Peptide), soluble Antibody |
102-PA21S |
ReliaTech |
100 µg |
EUR 126 |
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. |
Human VEGFR-2/KDR (D7), soluble Recombinant Protein |
S01-001 |
ReliaTech |
5 µg |
EUR 42 |
Description: Recombinant Human soluble Endothelial Growth Factor Receptor-2 (sKDR(D7)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein consists of all 7 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 116 kDa.Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Human VEGFR-2/KDR (D7), soluble Recombinant Protein |
S01-002 |
ReliaTech |
50 µg |
EUR 183.75 |
Description: Recombinant Human soluble Endothelial Growth Factor Receptor-2 (sKDR(D7)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein consists of all 7 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 116 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Human VEGFR-2/KDR (native), soluble Recombinant Protein |
S01-003 |
ReliaTech |
5 µg |
EUR 126 |
Description: The naturally occuring form of human soluble Endothelial Growth Factor Receptor-2 (sKDR) was cloned from a full length KDR cDNA by standard molecular methods. The soluble receptor protein consists of the first 6 extracellular domains and contains the unique C-terminal end of native human soluble VEGFR-2/KDR (CGRETILDHSAEAVGMP) generated by alternative splicing. The recombinant human sKDR is produced in a monomeric form in insect cells. The receptor monomers have a mass of approximately 105 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). For Flt-1 as well as KDR naturally occuring soluble forms are described. The expression of the receptors is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Human VEGFR-2/KDR (native), soluble Recombinant Protein |
S01-004 |
ReliaTech |
20 µg |
EUR 273 |
Description: The naturally occuring form of human soluble Endothelial Growth Factor Receptor-2 (sKDR) was cloned from a full length KDR cDNA by standard molecular methods. The soluble receptor protein consists of the first 6 extracellular domains and contains the unique C-terminal end of native human solubleVEGFR-2/KDR (CGRETILDHSAEAVGMP) generated by alternative splicing. The recombinant human sKDR is produced in a monomeric form in insect cells. The receptor monomers have a mass of approximately 105 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). For Flt-1 as well as KDR naturally occuring soluble forms are described. The expression of the receptors is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Human VEGFR-2/KDR-Fc Chimera, soluble Recombinant Protein |
SFC-007 |
ReliaTech |
10 µg |
EUR 57.75 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-2 (sVEGFR-2(D7)) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-2(D7)/Fc is a disulfide-linked homodimeric protein. The soluble receptor protein consists of all 7 extracellular domains (Met1-Ala757), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Human VEGFR-2/KDR-Fc Chimera, soluble Recombinant Protein |
SFC-008 |
ReliaTech |
50 µg |
EUR 168 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-2 (sVEGFR-2(D7)) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-2(D7)/Fc is a disulfide-linked homodimeric protein. The soluble receptor protein consists of all 7 extracellular domains (Met1-Ala757), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Anti-Human VEGFR1-14/Flt1-14 (peptide), soluble Antibody |
101-M29 |
ReliaTech |
100 µg |
EUR 199.5 |
Description: A human-specific splicing variant of vascular endothelial growth factor (VEGF) receptor 1 (Flt1) was discovered, producing a soluble receptor (designated sFlt1-14) that is qualitatively different from the previously described soluble receptor (sFlt1) and functioning as a potent VEGF inhibitor. sFlt1-14 is generated in a cell type-specific fashion, primarily in non-endothelial cells. Notably, in vascular smooth muscle cells, all Flt1 messenger RNA is converted to sFlt1-14, whereas endothelial cells of the same human vessel express sFlt1. sFlt1-14 expression by vascular smooth muscle cells is dynamically regulated as evidenced by its upregulation on coculture with endothelial cells or by direct exposure to VEGF. Increased production of soluble VEGF receptors during pregnancy is entirely attributable to induced expression of placental sFlt1-14 starting by the end of the first trimester. Expression is dramatically elevated in the placenta of women with preeclampsia, specifically induced in abnormal clusters of degenerative syncytiotrophoblasts known as syncytial knots, where it may undergo further messenger RNA editing. sFlt1-14 is the predominant VEGF-inhibiting protein produced by the preeclamptic placenta, accumulates in the circulation, and hence is capable of neutralizing VEGF in distant organs affected in preeclampsia. Together, these findings revealed a new natural VEGF inhibitor that has evolved in humans, possibly to protect non-endothelial cells from adverse VEGF signaling. Furthermore, the study uncovered the identity of a VEGF-blocking protein implicated in preeclampsia. |
VEGFR binding peptide KH / QKRKRKKSRKKH |
007-58 |
PHOENIX PEPTIDE |
100 μg |
EUR 158.76 |
VEGFR binding peptide IVLS / RKRKRKKSRYIVLS |
007-59 |
PHOENIX PEPTIDE |
100 μg |
EUR 171.72 |
VEGFR-KDR/Flk-1 Antagonist Peptide |
H-5896.0001 |
Bachem |
1.0mg |
EUR 691.2 |
Description: Sum Formula: C77H99N23O18S; CAS# [492444-99-2] net |
VEGFR-KDR/Flk-1 Antagonist Peptide |
H-5896.0005 |
Bachem |
5.0mg |
EUR 2648.4 |
Description: Sum Formula: C77H99N23O18S; CAS# [492444-99-2] net |
Human VEGFR-3/FLT-4, soluble Recombinant Protein |
S01-017 |
ReliaTech |
10 µg |
EUR 103.95 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis. |
Human VEGFR-3/FLT-4, soluble Recombinant Protein |
S01-017S |
ReliaTech |
5 µg |
EUR 63 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis. |
Human VEGFR-3/FLT-4, soluble Recombinant Protein |
S01-018 |
ReliaTech |
50 µg |
EUR 210 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23 aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751 aa residue extracellular domain, a 22 aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis. |
Human VEGFR-1/Flt-1 (D5), soluble Recombinant Protein |
S01-011 |
ReliaTech |
5 µg |
EUR 73.5 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-5 (sVEGFR-1(D5)) is a 70 kDa protein. The baculovirus generated, recombinant human sVEGFR-1 is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 70 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (D5), soluble Recombinant Protein |
S01-012 |
ReliaTech |
20 µg |
EUR 157.5 |
Description: Recombinat human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-5 (sVEGFR-1(D5)) is a 70 kDa protein containing amino acid residues. The baculovirus generated, recombinant human sVEGFR-1 is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 70 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (D4), soluble Recombinant Protein |
S01-013 |
ReliaTech |
5 µg |
EUR 103.95 |
Description: Recombinant Human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-4 (sVEGFR-1(D4)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 4 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 55 kDa containing 457 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (D4), soluble Recombinant Protein |
S01-014 |
ReliaTech |
20 µg |
EUR 199.5 |
Description: Recombinant Human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-4 (sVEGFR-1(D4)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 4 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 55 kDa containing 457 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (D3), soluble Recombinant Protein |
S01-015 |
ReliaTech |
5 µg |
EUR 103.95 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (D3), soluble Recombinant Protein |
S01-016 |
ReliaTech |
20 µg |
EUR 199.5 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (native), soluble Recombinant Protein |
S01-009 |
ReliaTech |
5 µg |
EUR 73.5 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1) is the naturally occurring form and was cloned from total RNA of human umbilical vein endothelial cells. The recombinant mature sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96 kDa. The soluble receptor precursor protein consists of the first 6 extracellular domains (Met1-His688) containing the unique 31 amino acids residues at the C-terminus. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly, a naturally occurring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (native), soluble Recombinant Protein |
S01-010 |
ReliaTech |
20 µg |
EUR 157.5 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1) is the naturally occurring form and was cloned from total RNA of human umbilical vein endothelial cells. The recombinant mature sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96 kDa. The soluble receptor protein consists of the first 6 extracellular domains (Met1-His688) containing the unique 31 amino acids residues at the C-terminus. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly, a naturally occurring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (D3)-His, soluble Recombinant Protein |
S01-080 |
ReliaTech |
50 µg |
EUR 378 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Soluble ST2 (Human) - ELISA Kit |
EK-036-10 |
PHOENIX PEPTIDE |
96 wells |
EUR 629.64 |
Human VEGFR-3/FLT-4/Fc Chimera, soluble Recombinant Protein |
SFC-009 |
ReliaTech |
10 µg |
EUR 73.5 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-3/Fc is a disulfide-linked homodimeric protein. The sVEGFR-3/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The VEGFR-3/FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The FLT-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial at latter stages of development. It is important for lymphangiogenesis. |
Human VEGFR-3/FLT-4/Fc Chimera, soluble Recombinant Protein |
SFC-010 |
ReliaTech |
50 µg |
EUR 189 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-3/Fc is a disulfide-linked homodimeric protein. The sVEGFR-3/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The VEGFR-3/FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The FLT-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial at latter stages of development. It is important for lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
102-PA18 |
ReliaTech |
200 µg |
EUR 204.75 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
102-PA18AG |
ReliaTech |
50 µg |
EUR 147 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
102-PA18S |
ReliaTech |
100 µg |
EUR 126 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
102-PABi18 |
ReliaTech |
50 µg |
EUR 157.5 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-M20 |
ReliaTech |
100 µg |
EUR 199.5 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-M22 |
ReliaTech |
100 µg |
EUR 246.75 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-M32 |
ReliaTech |
100 µg |
EUR 189 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-M34 |
ReliaTech |
100 µg |
EUR 189 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-M35 |
ReliaTech |
100 µg |
EUR 399 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-M35A |
ReliaTech |
100 µg |
EUR 399 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-MBi20 |
ReliaTech |
50 µg |
EUR 199.5 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-MBi22 |
ReliaTech |
50 µg |
EUR 246.75 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-MBi32 |
ReliaTech |
50 µg |
EUR 189 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-MBi34 |
ReliaTech |
50 µg |
EUR 189 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein |
SFC-005 |
ReliaTech |
10 µg |
EUR 57.75 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1(D7)) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1(D7)/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1(D7)/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein |
SFC-006 |
ReliaTech |
50 µg |
EUR 168 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1(D7)) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1(D7)/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1(D7)/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
KDR / VEGFR-2 |
E8RT1347 |
EnoGene |
100ul |
EUR 275 |
Description: Available in various conjugation types. |
Mouse VEGFR-2/Flk-1 (native), soluble Recombinant Protein |
S01-M03 |
ReliaTech |
5 µg |
EUR 126 |
Description: Disruption of the precise balance of positive and negative molecular regulators of blood and lymphatic vessel growth can lead to myriad diseases. Although dozens of natural inhibitors of hemangiogenesis have been identified, an endogenous selective inhibitor of lymphatic vessel growth has not to our knowledge been previously described. A splice variant of the gene encoding vascular endothelial growth factor receptor-2 (VEGFR-2) that encodes a secreted form of the protein, designated endogenous soluble VEGFR-2 (esVEGFR-2/KDR) has been described. The endogenous soluble esKDR inhibits developmental and reparative lymphangiogenesis by blocking VEGF-C function. Tissue-specific loss of esKDR in mice induced, at birth, spontaneous lymphatic invasion of the normally alymphatic cornea and hyperplasia of skin lymphatics without affecting blood vasculature. Administration of esKDR inhibited lymphangiogenesis but not hemangiogenesis induced by corneal suture injury or transplantation, enhanced corneal allograft survival and suppressed lymphangioma cellular proliferation. Naturally occurring esKDR thus acts as a molecular uncoupler of blood and lymphatic vessels; modulation of esKDR might have therapeutic effects in treating lymphatic vascular malformations, transplantation rejection and, potentially, tumor lymphangiogenesis and lymphedema. Recombinant human esKDR generated by alternative splicing consist of the first 6 Ig-like loops followed by the unique C-terminal end: GMEASLGDRIAMP. |
Mouse VEGFR-2/Flk-1 (native), soluble Recombinant Protein |
S01-M04 |
ReliaTech |
20 µg |
EUR 273 |
Description: Disruption of the precise balance of positive and negative molecular regulators of blood and lymphatic vessel growth can lead to myriad diseases. Although dozens of natural inhibitors of hemangiogenesis have been identified, an endogenous selective inhibitor of lymphatic vessel growth has not to our knowledge been previously described. A splice variant of the gene encoding vascular endothelial growth factor receptor-2 (VEGFR-2) that encodes a secreted form of the protein, designated endogenous soluble VEGFR-2 (esVEGFR-2/KDR) has been described. The endogenous soluble esKDR inhibits developmental and reparative lymphangiogenesis by blocking VEGF-C function. Tissue-specific loss of esKDR in mice induced, at birth, spontaneous lymphatic invasion of the normally alymphatic cornea and hyperplasia of skin lymphatics without affecting blood vasculature. Administration of esKDR inhibited lymphangiogenesis but not hemangiogenesis induced by corneal suture injury or transplantation, enhanced corneal allograft survival and suppressed lymphangioma cellular proliferation. Naturally occurring esKDR thus acts as a molecular uncoupler of blood and lymphatic vessels; modulation of esKDR might have therapeutic effects in treating lymphatic vascular malformations, transplantation rejection and, potentially, tumor lymphangiogenesis and lymphedema. Recombinant human esKDR generated by alternative splicing consist of the first 6 Ig-like loops followed by the unique C-terminal end: GMEASLGDRIAMP. |
KDR / VEGFR-2 Antibody |
48311 |
SAB |
100ul |
EUR 429 |
KDR / VEGFR-2 Antibody |
48311-100ul |
SAB |
100ul |
EUR 399.6 |
KDR / VEGFR-2 Antibody |
48311-50ul |
SAB |
50ul |
EUR 286.8 |
Human soluble vascular endothelial growth factor receptor-2(VEGFR-2/sFLK-1) Elisa Kit |
EK711423 |
AFG Bioscience LLC |
96 Wells |
EUR 0.17 |
Human soluble vascular endothelial growth factor receptor-2,VEGFR-2/sFLK-1 ELISA Kit |
CN-03788H1 |
ChemNorm |
96T |
EUR 576 |
Human soluble vascular endothelial growth factor receptor-2,VEGFR-2/sFLK-1 ELISA Kit |
CN-03788H2 |
ChemNorm |
48T |
EUR 397.2 |
Human soluble vascular endothelial growth factor receptor-2(VEGFR-2/sFLK-1) ELISA Kit |
NSL0270Hu |
Sunlong |
96 wells |
EUR 468 |
|
Human soluble vascular endothelial growth factor receptor-2,VEGFR-2/sFLK-1 ELISA Kit |
SL1627Hu |
Sunlong |
96 Tests |
EUR 468 |
|
Anti-Human VEGFR-2/KDR-FITC Antibody |
101-M20-FITC |
ReliaTech |
50 µg |
Ask for price |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR-FITC Antibody |
101-M20S-FITC |
ReliaTech |
25 µg |
Ask for price |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR, Agonistic Antibody |
mV1001.3m-h |
ReliaTech |
100 µg |
EUR 645.75 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. The antibody will bind near the ligand binding site of the receptor and has agonistic activity. |
Anti-Human VEGFR-2/KDR, Antagonistic Antibody |
mV1001.1m-h |
ReliaTech |
100 µg |
EUR 645.75 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. The antibody will bind near the ligand binding site of the receptor and has antagonistic activity by blocking the binding of natural ligands. |
Human Soluble Mesothelin Related Peptide(SMRP) Elisa Kit |
EK714587 |
AFG Bioscience LLC |
96 Wells |
EUR 0.47 |
Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit |
EKF57716-48T |
Biomatik Corporation |
48T |
EUR 396.9 |
Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit |
EKF57716-5x96T |
Biomatik Corporation |
5x96T |
EUR 2693.25 |
Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit |
EKF57716-96T |
Biomatik Corporation |
96T |
EUR 567 |
Human SMRP (Soluble Mesothelin Related Peptide) ELISA Kit |
EKE61404-5x96T |
Biomatik Corporation |
5x96T |
EUR 3124.08 |
Human SMRP (Soluble Mesothelin Related Peptide) ELISA Kit |
EKE61404-96T |
Biomatik Corporation |
96T |
EUR 657.7 |
Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit |
EH3796 |
FN Test |
96T |
EUR 628.92 |
- Detection range: 0.313-20pmol/ml
- Alias: SMRP/Soluble Mesothelin Related Peptide
|
Description: Method of detection: Double Antibody, Sandwich ELISA;Reacts with: Homo sapiens;Sensitivity: 0.188pmol/ml |
Human Soluble Mesothelin Related Peptide(SMRP)ELISA Kit |
CSB-E13725h-24T |
Cusabio |
1 plate of 24 wells |
EUR 198 |
- Sample volume: 50-100ul
- Detection wavelength: 450nm
- Assay performance time: 1 to 4 hours.
|
Description: Quantitativesandwich ELISA kit for measuring Human Soluble Mesothelin Related Peptide (SMRP) in samples from serum, plasma, tissue homogenates, cell lysates. A new trial version of the kit, which allows you to test the kit in your application at a reasonable price. |
Human Soluble Mesothelin Related Peptide(SMRP)ELISA Kit |
1-CSB-E13725h |
Cusabio |
-
Ask for price
-
Ask for price
-
Ask for price
|
-
1 plate of 96 wells
-
10 plates of 96 wells each
-
5 plates of 96 wells each
|
- Sample volume: 50-100ul
- Detection wavelength: 450nm
- Assay performance time: 1 to 4 hours.
|
Description: Quantitativesandwich ELISA kit for measuring Human Soluble Mesothelin Related Peptide(SMRP) in samples from serum, plasma, tissue homogenates, cell lysates. Now available in a cost efficient pack of 5 plates of 96 wells each, conveniently packed along with the other reagents in 5 separate kits. |
Human Soluble Mesothelin Related Peptide (SMRP) ELISA Kit |
abx253186-96tests |
Abbexa |
96 tests |
EUR 848.4 |
- Shipped within 5-12 working days.
|
Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit |
RE2600H-48wells |
Reed Biotech |
48 wells |
EUR 116.55 |
- Research Area: Enzyme & Kinase
|
Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit |
RE2600H-96wells |
Reed Biotech |
96 wells |
EUR 161.55 |
- Research Area: Enzyme & Kinase
|
Human Soluble Mesothelin Related Peptide, SMRP ELISA Kit |
SELI-66010h |
Lifescience Market |
96 Tests |
EUR 788.4 |
Human Soluble Mesothelin Related Peptide,SMRP ELISA Kit |
YLA0424HU-48T |
Shanghai YL Biotech |
48T |
Ask for price |
Human Soluble Mesothelin Related Peptide,SMRP ELISA Kit |
YLA0424HU-96T |
Shanghai YL Biotech |
96T |
Ask for price |
Human FLT-4/VEGFR-3 control/blocking peptide #2 |
FLT42-P |
Alpha Diagnostics |
100 ug |
EUR 196.8 |
Human Soluble Vascular endothelial cell growth factor receptor 1 (VEGFR-1) ELISA Kit |
EK5866 |
SAB |
96Т |
EUR 799 |
- http://www.sabbiotech.com/g-153196-Human-Soluble-Vascular-endothelial-cell-growth-factor-receptor-1-(VEGFR-1)-ELISA-Kit-EK5866.html
|
Human Soluble Vascular endothelial cell growth factor receptor 1 (VEGFR-1) ELISA Kit |
AE11708HU-48Tests |
Abebio |
48 Tests |
EUR 290 |
|
Description: Human (Homo sapiens) |
Human Soluble Vascular endothelial cell growth factor receptor 1 (VEGFR-1) ELISA Kit |
AE11708HU-96Tests |
Abebio |
96 Tests |
EUR 540 |
|
Description: Human (Homo sapiens) |
Anti-Mouse VEGFR-2/KDR, Agonistic Antibody |
mV1001r-m |
ReliaTech |
100 µg |
EUR 645.75 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. The antibody will bind near the ligand binding site of the receptor and has agonistic activity. |
Human Soluble Mesothelin Related Peptide, SMRP GENLISA ELISA |
KBH3303 |
Krishgen |
1 x 96 wells |
EUR 286 |
Anti-Mouse VEGFR-2/KDR, Antagonistic Antibody |
mV1001.1r-m |
ReliaTech |
100 µg |
EUR 645.75 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. The antibody will bind near the ligand binding site of the receptor and has antagonistic activity by blocking the binding of natural ligands. |
KDR / VEGFR-2 Conjugated Antibody |
C48311 |
SAB |
100ul |
EUR 476.4 |
ELISA kit for Human SMRP (Soluble Mesothelin Related Peptide) |
E-EL-H5488 |
Elabscience Biotech |
1 plate of 96 wells |
EUR 640.8 |
- Gentaur's SMRP ELISA kit utilizes the Sandwich-ELISA principle. The micro ELISA plate provided in this kit has been pre-coated with an antibody specific to Human SMRP. Standards or samples are added to the micro ELISA plate wells and combined with th
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Description: A sandwich ELISA kit for quantitative measurement of Human SMRP (Soluble Mesothelin Related Peptide) in samples from Serum, Plasma, Cell supernatant |
Mouse VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein |
SFC-M05 |
ReliaTech |
10 µg |
EUR 57.75 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1D1-7) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1D1-7/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1D1-7/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Mouse VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein |
SFC-M06 |
ReliaTech |
50 µg |
EUR 168 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1D1-7) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1D1-7/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1D1-7/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Pig Soluble vascular endothelial growth factor receptor-2 (VEGFR-2/sFLK-1) ELISA Kit |
EK12217 |
SAB |
96Т |
EUR 799 |
- http://www.sabbiotech.com/g-159547-Pig-Soluble-vascular-endothelial-growth-factor-receptor-2-(VEGFR-2/sFLK-1)-ELISA-Kit-EK12217.html
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Pig Soluble vascular endothelial growth factor receptor-2 (VEGFR-2/sFLK-1) ELISA Kit |
AE63268PI-48Tests |
Abebio |
48 Tests |
EUR 360 |
|
Description: Pig (Sus scrofa; Porcine) |
Pig Soluble vascular endothelial growth factor receptor-2 (VEGFR-2/sFLK-1) ELISA Kit |
AE63268PI-96Tests |
Abebio |
96 Tests |
EUR 680 |
|
Description: Pig (Sus scrofa; Porcine) |
Mouse Soluble Vascular Endothelial Growth Factor Receptor 2(VEGFR-2/sFLK-1)ELISA kit |
GA-E0616MS-48T |
GenAsia Biotech |
48T |
EUR 403.2 |
Mouse Soluble Vascular Endothelial Growth Factor Receptor 2(VEGFR-2/sFLK-1)ELISA kit |
GA-E0616MS-96T |
GenAsia Biotech |
96T |
EUR 640.8 |
Improved survival with ipilimumab in victims with metastatic melanoma.
BACKGROUND
An enchancment usually survival amongst victims with metastatic melanoma has been an elusive goal. On this part Three analysis, ipilimumab–which blocks cytotoxic T-lymphocyte-associated antigen 4 to potentiate an antitumor T-cell response–administered with or with no glycoprotein 100 (gp100) peptide vaccine was in distinction with gp100 alone in victims with beforehand dealt with metastatic melanoma.
METHODS
A whole of 676 HLA-A*0201-positive victims with unresectable stage III or IV melanoma, whose sickness had progressed whereas they’d been receiving treatment for metastatic sickness, had been randomly assigned, in a 3:1:1 ratio, to acquire ipilimumab plus gp100 (403 victims), ipilimumab alone (137), or gp100 alone (136).
Ipilimumab, at a dose of three mg per kilogram of physique weight, was administered with or with out gp100 every Three weeks for as a lot as four cures (induction). Eligible victims might acquire reinduction treatment. The primary end stage was normal survival.
RESULTS
The median normal survival was 10.Zero months amongst victims receiving ipilimumab plus gp100, as in distinction with 6.4 months amongst victims receiving gp100 alone (hazard ratio for lack of life, 0.68; P<0.001). The median normal survival with ipilimumab alone was 10.1 months (hazard ratio for lack of life inside the comparability with gp100 alone, 0.66; P=0.003).
No distinction usually survival was detected between the ipilimumab groups (hazard ratio with ipilimumab plus gp100, 1.04; P=0.76). Grade Three or 4 immune-related hostile events occurred in 10 to 15% of victims dealt with with ipilimumab and in 3% dealt with with gp100 alone. There have been 14 deaths related to the analysis medicine (2.1%), and 7 had been associated with immune-related hostile events.
CONCLUSIONS
Ipilimumab, with or with no gp100 peptide vaccine, as in distinction with gp100 alone, improved normal survival in victims with beforehand dealt with metastatic melanoma.
Adversarial events may be excessive, long-lasting, or every, nevertheless most are reversible with relevant treatment. (Funded by Medarex and Bristol-Myers Squibb; ClinicalTrials.gov amount, NCT00094653.)
Anti-Mouse VEGFR-2/Flk-1 (Peptide), soluble Antibody |
103-PA19 |
ReliaTech |
200 µg |
EUR 204.75 |
Description: The antibody recognizes solely the endogenous soluble form of mouse vascular endothelial growth factor receptor 2, alos known as CD309, VEGFR2, KDR, protein tyrosine kinase receptor flk-1, and fetal liver kinase-1. The endogenous soluble mouse esFlk-1 generated by alternative splicing consists of the first 6 Ig-like loops followed by the unique C-terminal end: GMEASLGDRIAMP. Flk-1 is a member of the tyrosine protein kinase family, sub-family CSF-1/PDGF, that contains a single pass transmembrane receptor with a protein kinase domain and seven immunoglobulin-like domains in the extracellular region. Flk-1 is expressed at high levels in adult heart, lung, kidney, brain, and skeletal muscle; other tissues express at lower levels. Flk-1 is a receptor for VEGF-A or fully processed VEGF-C; ligand binding plays a key role in vascular development and vascular permeability. |
Anti-Mouse VEGFR-2/Flk-1 (Peptide), soluble Antibody |
103-PA19S |
ReliaTech |
100 µg |
EUR 126 |
Description: The antibody recognizes solely the endogenous soluble form of mouse vascular endothelial growth factor receptor 2, alos known as CD309, VEGFR2, KDR, protein tyrosine kinase receptor flk-1, and fetal liver kinase-1. The endogenous soluble mouse esFlk-1 generated by alternative splicing consists of the first 6 Ig-like loops followed by the unique C-terminal end: GMEASLGDRIAMP. Flk-1 is a member of the tyrosine protein kinase family, sub-family CSF-1/PDGF, that contains a single pass transmembrane receptor with a protein kinase domain and seven immunoglobulin-like domains in the extracellular region. Flk-1 is expressed at high levels in adult heart, lung, kidney, brain, and skeletal muscle; other tissues express at lower levels. Flk-1 is a receptor for VEGF-A or fully processed VEGF-C; ligand binding plays a key role in vascular development and vascular permeability. |
Anti-Human VEGFR-1/Flt-1 (Peptide), soluble Antibody |
102-PA21 |
ReliaTech |
200 µg |
EUR 204.75 |
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. |
Anti-Human VEGFR-1/Flt-1 (Peptide), soluble Antibody |
102-PA21S |
ReliaTech |
100 µg |
EUR 126 |
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. |
Human VEGFR-2/KDR (D7), soluble Recombinant Protein |
S01-001 |
ReliaTech |
5 µg |
EUR 42 |
Description: Recombinant Human soluble Endothelial Growth Factor Receptor-2 (sKDR(D7)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein consists of all 7 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 116 kDa.Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Human VEGFR-2/KDR (D7), soluble Recombinant Protein |
S01-002 |
ReliaTech |
50 µg |
EUR 183.75 |
Description: Recombinant Human soluble Endothelial Growth Factor Receptor-2 (sKDR(D7)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein consists of all 7 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 116 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Human VEGFR-2/KDR (native), soluble Recombinant Protein |
S01-003 |
ReliaTech |
5 µg |
EUR 126 |
Description: The naturally occuring form of human soluble Endothelial Growth Factor Receptor-2 (sKDR) was cloned from a full length KDR cDNA by standard molecular methods. The soluble receptor protein consists of the first 6 extracellular domains and contains the unique C-terminal end of native human soluble VEGFR-2/KDR (CGRETILDHSAEAVGMP) generated by alternative splicing. The recombinant human sKDR is produced in a monomeric form in insect cells. The receptor monomers have a mass of approximately 105 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). For Flt-1 as well as KDR naturally occuring soluble forms are described. The expression of the receptors is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Human VEGFR-2/KDR (native), soluble Recombinant Protein |
S01-004 |
ReliaTech |
20 µg |
EUR 273 |
Description: The naturally occuring form of human soluble Endothelial Growth Factor Receptor-2 (sKDR) was cloned from a full length KDR cDNA by standard molecular methods. The soluble receptor protein consists of the first 6 extracellular domains and contains the unique C-terminal end of native human solubleVEGFR-2/KDR (CGRETILDHSAEAVGMP) generated by alternative splicing. The recombinant human sKDR is produced in a monomeric form in insect cells. The receptor monomers have a mass of approximately 105 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). For Flt-1 as well as KDR naturally occuring soluble forms are described. The expression of the receptors is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Human VEGFR-2/KDR-Fc Chimera, soluble Recombinant Protein |
SFC-007 |
ReliaTech |
10 µg |
EUR 57.75 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-2 (sVEGFR-2(D7)) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-2(D7)/Fc is a disulfide-linked homodimeric protein. The soluble receptor protein consists of all 7 extracellular domains (Met1-Ala757), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Human VEGFR-2/KDR-Fc Chimera, soluble Recombinant Protein |
SFC-008 |
ReliaTech |
50 µg |
EUR 168 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-2 (sVEGFR-2(D7)) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-2(D7)/Fc is a disulfide-linked homodimeric protein. The soluble receptor protein consists of all 7 extracellular domains (Met1-Ala757), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Anti-Human VEGFR1-14/Flt1-14 (peptide), soluble Antibody |
101-M29 |
ReliaTech |
100 µg |
EUR 199.5 |
Description: A human-specific splicing variant of vascular endothelial growth factor (VEGF) receptor 1 (Flt1) was discovered, producing a soluble receptor (designated sFlt1-14) that is qualitatively different from the previously described soluble receptor (sFlt1) and functioning as a potent VEGF inhibitor. sFlt1-14 is generated in a cell type-specific fashion, primarily in non-endothelial cells. Notably, in vascular smooth muscle cells, all Flt1 messenger RNA is converted to sFlt1-14, whereas endothelial cells of the same human vessel express sFlt1. sFlt1-14 expression by vascular smooth muscle cells is dynamically regulated as evidenced by its upregulation on coculture with endothelial cells or by direct exposure to VEGF. Increased production of soluble VEGF receptors during pregnancy is entirely attributable to induced expression of placental sFlt1-14 starting by the end of the first trimester. Expression is dramatically elevated in the placenta of women with preeclampsia, specifically induced in abnormal clusters of degenerative syncytiotrophoblasts known as syncytial knots, where it may undergo further messenger RNA editing. sFlt1-14 is the predominant VEGF-inhibiting protein produced by the preeclamptic placenta, accumulates in the circulation, and hence is capable of neutralizing VEGF in distant organs affected in preeclampsia. Together, these findings revealed a new natural VEGF inhibitor that has evolved in humans, possibly to protect non-endothelial cells from adverse VEGF signaling. Furthermore, the study uncovered the identity of a VEGF-blocking protein implicated in preeclampsia. |
VEGFR binding peptide KH / QKRKRKKSRKKH |
007-58 |
PHOENIX PEPTIDE |
100 μg |
EUR 158.76 |
VEGFR binding peptide IVLS / RKRKRKKSRYIVLS |
007-59 |
PHOENIX PEPTIDE |
100 μg |
EUR 171.72 |
VEGFR-KDR/Flk-1 Antagonist Peptide |
H-5896.0001 |
Bachem |
1.0mg |
EUR 691.2 |
Description: Sum Formula: C77H99N23O18S; CAS# [492444-99-2] net |
VEGFR-KDR/Flk-1 Antagonist Peptide |
H-5896.0005 |
Bachem |
5.0mg |
EUR 2648.4 |
Description: Sum Formula: C77H99N23O18S; CAS# [492444-99-2] net |
Human VEGFR-3/FLT-4, soluble Recombinant Protein |
S01-017 |
ReliaTech |
10 µg |
EUR 103.95 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis. |
Human VEGFR-3/FLT-4, soluble Recombinant Protein |
S01-017S |
ReliaTech |
5 µg |
EUR 63 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis. |
Human VEGFR-3/FLT-4, soluble Recombinant Protein |
S01-018 |
ReliaTech |
50 µg |
EUR 210 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23 aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751 aa residue extracellular domain, a 22 aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis. |
Human VEGFR-1/Flt-1 (D5), soluble Recombinant Protein |
S01-011 |
ReliaTech |
5 µg |
EUR 73.5 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-5 (sVEGFR-1(D5)) is a 70 kDa protein. The baculovirus generated, recombinant human sVEGFR-1 is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 70 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (D5), soluble Recombinant Protein |
S01-012 |
ReliaTech |
20 µg |
EUR 157.5 |
Description: Recombinat human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-5 (sVEGFR-1(D5)) is a 70 kDa protein containing amino acid residues. The baculovirus generated, recombinant human sVEGFR-1 is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 70 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (D4), soluble Recombinant Protein |
S01-013 |
ReliaTech |
5 µg |
EUR 103.95 |
Description: Recombinant Human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-4 (sVEGFR-1(D4)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 4 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 55 kDa containing 457 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (D4), soluble Recombinant Protein |
S01-014 |
ReliaTech |
20 µg |
EUR 199.5 |
Description: Recombinant Human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-4 (sVEGFR-1(D4)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 4 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 55 kDa containing 457 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (D3), soluble Recombinant Protein |
S01-015 |
ReliaTech |
5 µg |
EUR 103.95 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (D3), soluble Recombinant Protein |
S01-016 |
ReliaTech |
20 µg |
EUR 199.5 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (native), soluble Recombinant Protein |
S01-009 |
ReliaTech |
5 µg |
EUR 73.5 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1) is the naturally occurring form and was cloned from total RNA of human umbilical vein endothelial cells. The recombinant mature sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96 kDa. The soluble receptor precursor protein consists of the first 6 extracellular domains (Met1-His688) containing the unique 31 amino acids residues at the C-terminus. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly, a naturally occurring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (native), soluble Recombinant Protein |
S01-010 |
ReliaTech |
20 µg |
EUR 157.5 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1) is the naturally occurring form and was cloned from total RNA of human umbilical vein endothelial cells. The recombinant mature sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96 kDa. The soluble receptor protein consists of the first 6 extracellular domains (Met1-His688) containing the unique 31 amino acids residues at the C-terminus. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly, a naturally occurring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (D3)-His, soluble Recombinant Protein |
S01-080 |
ReliaTech |
50 µg |
EUR 378 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Soluble ST2 (Human) - ELISA Kit |
EK-036-10 |
PHOENIX PEPTIDE |
96 wells |
EUR 629.64 |
Human VEGFR-3/FLT-4/Fc Chimera, soluble Recombinant Protein |
SFC-009 |
ReliaTech |
10 µg |
EUR 73.5 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-3/Fc is a disulfide-linked homodimeric protein. The sVEGFR-3/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The VEGFR-3/FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The FLT-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial at latter stages of development. It is important for lymphangiogenesis. |
Human VEGFR-3/FLT-4/Fc Chimera, soluble Recombinant Protein |
SFC-010 |
ReliaTech |
50 µg |
EUR 189 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-3/Fc is a disulfide-linked homodimeric protein. The sVEGFR-3/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The VEGFR-3/FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The FLT-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial at latter stages of development. It is important for lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
102-PA18 |
ReliaTech |
200 µg |
EUR 204.75 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
102-PA18AG |
ReliaTech |
50 µg |
EUR 147 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
102-PA18S |
ReliaTech |
100 µg |
EUR 126 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
102-PABi18 |
ReliaTech |
50 µg |
EUR 157.5 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-M20 |
ReliaTech |
100 µg |
EUR 199.5 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-M22 |
ReliaTech |
100 µg |
EUR 246.75 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-M32 |
ReliaTech |
100 µg |
EUR 189 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-M34 |
ReliaTech |
100 µg |
EUR 189 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-M35 |
ReliaTech |
100 µg |
EUR 399 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-M35A |
ReliaTech |
100 µg |
EUR 399 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-MBi20 |
ReliaTech |
50 µg |
EUR 199.5 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-MBi22 |
ReliaTech |
50 µg |
EUR 246.75 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-MBi32 |
ReliaTech |
50 µg |
EUR 189 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR Antibody |
101-MBi34 |
ReliaTech |
50 µg |
EUR 189 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein |
SFC-005 |
ReliaTech |
10 µg |
EUR 57.75 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1(D7)) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1(D7)/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1(D7)/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein |
SFC-006 |
ReliaTech |
50 µg |
EUR 168 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1(D7)) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1(D7)/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1(D7)/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
KDR / VEGFR-2 |
E8RT1347 |
EnoGene |
100ul |
EUR 275 |
Description: Available in various conjugation types. |
Mouse VEGFR-2/Flk-1 (native), soluble Recombinant Protein |
S01-M03 |
ReliaTech |
5 µg |
EUR 126 |
Description: Disruption of the precise balance of positive and negative molecular regulators of blood and lymphatic vessel growth can lead to myriad diseases. Although dozens of natural inhibitors of hemangiogenesis have been identified, an endogenous selective inhibitor of lymphatic vessel growth has not to our knowledge been previously described. A splice variant of the gene encoding vascular endothelial growth factor receptor-2 (VEGFR-2) that encodes a secreted form of the protein, designated endogenous soluble VEGFR-2 (esVEGFR-2/KDR) has been described. The endogenous soluble esKDR inhibits developmental and reparative lymphangiogenesis by blocking VEGF-C function. Tissue-specific loss of esKDR in mice induced, at birth, spontaneous lymphatic invasion of the normally alymphatic cornea and hyperplasia of skin lymphatics without affecting blood vasculature. Administration of esKDR inhibited lymphangiogenesis but not hemangiogenesis induced by corneal suture injury or transplantation, enhanced corneal allograft survival and suppressed lymphangioma cellular proliferation. Naturally occurring esKDR thus acts as a molecular uncoupler of blood and lymphatic vessels; modulation of esKDR might have therapeutic effects in treating lymphatic vascular malformations, transplantation rejection and, potentially, tumor lymphangiogenesis and lymphedema. Recombinant human esKDR generated by alternative splicing consist of the first 6 Ig-like loops followed by the unique C-terminal end: GMEASLGDRIAMP. |
Mouse VEGFR-2/Flk-1 (native), soluble Recombinant Protein |
S01-M04 |
ReliaTech |
20 µg |
EUR 273 |
Description: Disruption of the precise balance of positive and negative molecular regulators of blood and lymphatic vessel growth can lead to myriad diseases. Although dozens of natural inhibitors of hemangiogenesis have been identified, an endogenous selective inhibitor of lymphatic vessel growth has not to our knowledge been previously described. A splice variant of the gene encoding vascular endothelial growth factor receptor-2 (VEGFR-2) that encodes a secreted form of the protein, designated endogenous soluble VEGFR-2 (esVEGFR-2/KDR) has been described. The endogenous soluble esKDR inhibits developmental and reparative lymphangiogenesis by blocking VEGF-C function. Tissue-specific loss of esKDR in mice induced, at birth, spontaneous lymphatic invasion of the normally alymphatic cornea and hyperplasia of skin lymphatics without affecting blood vasculature. Administration of esKDR inhibited lymphangiogenesis but not hemangiogenesis induced by corneal suture injury or transplantation, enhanced corneal allograft survival and suppressed lymphangioma cellular proliferation. Naturally occurring esKDR thus acts as a molecular uncoupler of blood and lymphatic vessels; modulation of esKDR might have therapeutic effects in treating lymphatic vascular malformations, transplantation rejection and, potentially, tumor lymphangiogenesis and lymphedema. Recombinant human esKDR generated by alternative splicing consist of the first 6 Ig-like loops followed by the unique C-terminal end: GMEASLGDRIAMP. |
KDR / VEGFR-2 Antibody |
48311 |
SAB |
100ul |
EUR 429 |
KDR / VEGFR-2 Antibody |
48311-100ul |
SAB |
100ul |
EUR 399.6 |
KDR / VEGFR-2 Antibody |
48311-50ul |
SAB |
50ul |
EUR 286.8 |
Human soluble vascular endothelial growth factor receptor-2(VEGFR-2/sFLK-1) Elisa Kit |
EK711423 |
AFG Bioscience LLC |
96 Wells |
EUR 0.17 |
Human soluble vascular endothelial growth factor receptor-2,VEGFR-2/sFLK-1 ELISA Kit |
CN-03788H1 |
ChemNorm |
96T |
EUR 576 |
Human soluble vascular endothelial growth factor receptor-2,VEGFR-2/sFLK-1 ELISA Kit |
CN-03788H2 |
ChemNorm |
48T |
EUR 397.2 |
Human soluble vascular endothelial growth factor receptor-2(VEGFR-2/sFLK-1) ELISA Kit |
NSL0270Hu |
Sunlong |
96 wells |
EUR 468 |
|
Human soluble vascular endothelial growth factor receptor-2,VEGFR-2/sFLK-1 ELISA Kit |
SL1627Hu |
Sunlong |
96 Tests |
EUR 468 |
|
Anti-Human VEGFR-2/KDR-FITC Antibody |
101-M20-FITC |
ReliaTech |
50 µg |
Ask for price |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR-FITC Antibody |
101-M20S-FITC |
ReliaTech |
25 µg |
Ask for price |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. |
Anti-Human VEGFR-2/KDR, Agonistic Antibody |
mV1001.3m-h |
ReliaTech |
100 µg |
EUR 645.75 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. The antibody will bind near the ligand binding site of the receptor and has agonistic activity. |
Anti-Human VEGFR-2/KDR, Antagonistic Antibody |
mV1001.1m-h |
ReliaTech |
100 µg |
EUR 645.75 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. The antibody will bind near the ligand binding site of the receptor and has antagonistic activity by blocking the binding of natural ligands. |
Human Soluble Mesothelin Related Peptide(SMRP) Elisa Kit |
EK714587 |
AFG Bioscience LLC |
96 Wells |
EUR 0.47 |
Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit |
EKF57716-48T |
Biomatik Corporation |
48T |
EUR 396.9 |
Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit |
EKF57716-5x96T |
Biomatik Corporation |
5x96T |
EUR 2693.25 |
Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit |
EKF57716-96T |
Biomatik Corporation |
96T |
EUR 567 |
Human SMRP (Soluble Mesothelin Related Peptide) ELISA Kit |
EKE61404-5x96T |
Biomatik Corporation |
5x96T |
EUR 3124.08 |
Human SMRP (Soluble Mesothelin Related Peptide) ELISA Kit |
EKE61404-96T |
Biomatik Corporation |
96T |
EUR 657.7 |
Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit |
EH3796 |
FN Test |
96T |
EUR 628.92 |
- Detection range: 0.313-20pmol/ml
- Alias: SMRP/Soluble Mesothelin Related Peptide
|
Description: Method of detection: Double Antibody, Sandwich ELISA;Reacts with: Homo sapiens;Sensitivity: 0.188pmol/ml |
Human Soluble Mesothelin Related Peptide(SMRP)ELISA Kit |
CSB-E13725h-24T |
Cusabio |
1 plate of 24 wells |
EUR 198 |
- Sample volume: 50-100ul
- Detection wavelength: 450nm
- Assay performance time: 1 to 4 hours.
|
Description: Quantitativesandwich ELISA kit for measuring Human Soluble Mesothelin Related Peptide (SMRP) in samples from serum, plasma, tissue homogenates, cell lysates. A new trial version of the kit, which allows you to test the kit in your application at a reasonable price. |
Human Soluble Mesothelin Related Peptide(SMRP)ELISA Kit |
1-CSB-E13725h |
Cusabio |
-
Ask for price
-
Ask for price
-
Ask for price
|
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1 plate of 96 wells
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10 plates of 96 wells each
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5 plates of 96 wells each
|
- Sample volume: 50-100ul
- Detection wavelength: 450nm
- Assay performance time: 1 to 4 hours.
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Description: Quantitativesandwich ELISA kit for measuring Human Soluble Mesothelin Related Peptide(SMRP) in samples from serum, plasma, tissue homogenates, cell lysates. Now available in a cost efficient pack of 5 plates of 96 wells each, conveniently packed along with the other reagents in 5 separate kits. |
Human Soluble Mesothelin Related Peptide (SMRP) ELISA Kit |
abx253186-96tests |
Abbexa |
96 tests |
EUR 848.4 |
- Shipped within 5-12 working days.
|
Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit |
RE2600H-48wells |
Reed Biotech |
48 wells |
EUR 116.55 |
- Research Area: Enzyme & Kinase
|
Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit |
RE2600H-96wells |
Reed Biotech |
96 wells |
EUR 161.55 |
- Research Area: Enzyme & Kinase
|
Human Soluble Mesothelin Related Peptide, SMRP ELISA Kit |
SELI-66010h |
Lifescience Market |
96 Tests |
EUR 788.4 |
Human Soluble Mesothelin Related Peptide,SMRP ELISA Kit |
YLA0424HU-48T |
Shanghai YL Biotech |
48T |
Ask for price |
Human Soluble Mesothelin Related Peptide,SMRP ELISA Kit |
YLA0424HU-96T |
Shanghai YL Biotech |
96T |
Ask for price |
Human FLT-4/VEGFR-3 control/blocking peptide #2 |
FLT42-P |
Alpha Diagnostics |
100 ug |
EUR 196.8 |
Human Soluble Vascular endothelial cell growth factor receptor 1 (VEGFR-1) ELISA Kit |
EK5866 |
SAB |
96Т |
EUR 799 |
- http://www.sabbiotech.com/g-153196-Human-Soluble-Vascular-endothelial-cell-growth-factor-receptor-1-(VEGFR-1)-ELISA-Kit-EK5866.html
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Human Soluble Vascular endothelial cell growth factor receptor 1 (VEGFR-1) ELISA Kit |
AE11708HU-48Tests |
Abebio |
48 Tests |
EUR 290 |
|
Description: Human (Homo sapiens) |
Human Soluble Vascular endothelial cell growth factor receptor 1 (VEGFR-1) ELISA Kit |
AE11708HU-96Tests |
Abebio |
96 Tests |
EUR 540 |
|
Description: Human (Homo sapiens) |
Anti-Mouse VEGFR-2/KDR, Agonistic Antibody |
mV1001r-m |
ReliaTech |
100 µg |
EUR 645.75 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. The antibody will bind near the ligand binding site of the receptor and has agonistic activity. |
Human Soluble Mesothelin Related Peptide, SMRP GENLISA ELISA |
KBH3303 |
Krishgen |
1 x 96 wells |
EUR 286 |
Anti-Mouse VEGFR-2/KDR, Antagonistic Antibody |
mV1001.1r-m |
ReliaTech |
100 µg |
EUR 645.75 |
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis. The antibody will bind near the ligand binding site of the receptor and has antagonistic activity by blocking the binding of natural ligands. |
KDR / VEGFR-2 Conjugated Antibody |
C48311 |
SAB |
100ul |
EUR 476.4 |
ELISA kit for Human SMRP (Soluble Mesothelin Related Peptide) |
E-EL-H5488 |
Elabscience Biotech |
1 plate of 96 wells |
EUR 640.8 |
- Gentaur's SMRP ELISA kit utilizes the Sandwich-ELISA principle. The micro ELISA plate provided in this kit has been pre-coated with an antibody specific to Human SMRP. Standards or samples are added to the micro ELISA plate wells and combined with th
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Description: A sandwich ELISA kit for quantitative measurement of Human SMRP (Soluble Mesothelin Related Peptide) in samples from Serum, Plasma, Cell supernatant |
Mouse VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein |
SFC-M05 |
ReliaTech |
10 µg |
EUR 57.75 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1D1-7) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1D1-7/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1D1-7/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Mouse VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein |
SFC-M06 |
ReliaTech |
50 µg |
EUR 168 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1D1-7) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1D1-7/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1D1-7/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Pig Soluble vascular endothelial growth factor receptor-2 (VEGFR-2/sFLK-1) ELISA Kit |
EK12217 |
SAB |
96Т |
EUR 799 |
- http://www.sabbiotech.com/g-159547-Pig-Soluble-vascular-endothelial-growth-factor-receptor-2-(VEGFR-2/sFLK-1)-ELISA-Kit-EK12217.html
|
Pig Soluble vascular endothelial growth factor receptor-2 (VEGFR-2/sFLK-1) ELISA Kit |
AE63268PI-48Tests |
Abebio |
48 Tests |
EUR 360 |
|
Description: Pig (Sus scrofa; Porcine) |
Pig Soluble vascular endothelial growth factor receptor-2 (VEGFR-2/sFLK-1) ELISA Kit |
AE63268PI-96Tests |
Abebio |
96 Tests |
EUR 680 |
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Description: Pig (Sus scrofa; Porcine) |
Mouse Soluble Vascular Endothelial Growth Factor Receptor 2(VEGFR-2/sFLK-1)ELISA kit |
GA-E0616MS-48T |
GenAsia Biotech |
48T |
EUR 403.2 |
Mouse Soluble Vascular Endothelial Growth Factor Receptor 2(VEGFR-2/sFLK-1)ELISA kit |
GA-E0616MS-96T |
GenAsia Biotech |
96T |
EUR 640.8 |
Mouse Soluble Vascular Endothelial Growth Factor Receptor 2(VEGFR-2/sFLK-1)ELISA kit |
YLA0353MO-48T |
Shanghai YL Biotech |
48T |
Ask for price |
Mouse Soluble Vascular Endothelial Growth Factor Receptor 2(VEGFR-2/sFLK-1)ELISA kit |
YLA0353MO-96T |
Shanghai YL Biotech |
96T |
Ask for price |
Porcine soluble vascular endothelial growth factor receptor-2,VEGFR-2/sFLK-1 Elisa Kit |
EK751085 |
AFG Bioscience LLC |
96 Wells |
EUR 0.88 |
PoFAine soluble vascular endothelial growth factor receptor-2,VEGFR-2/sFLK-1 ELISA Kit |
CN-01287P1 |
ChemNorm |
96T |
EUR 590.4 |