All-atom empirical potential for molecular modeling and dynamics studies of proteins.

microbiologystudents
  1. 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 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 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 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 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 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 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 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 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 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

007-58 100 μg
EUR 158.76

VEGFR binding peptide IVLS / RKRKRKKSRYIVLS

007-59 100 μg
EUR 171.72

VEGFR-KDR/Flk-1 Antagonist Peptide

H-5896.0001 1.0mg
EUR 691.2
Description: Sum Formula: C77H99N23O18S; CAS# [492444-99-2] net

VEGFR-KDR/Flk-1 Antagonist Peptide

H-5896.0005 5.0mg
EUR 2648.4
Description: Sum Formula: C77H99N23O18S; CAS# [492444-99-2] net

Human VEGFR-3/FLT-4, soluble Recombinant Protein

S01-017 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 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 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 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 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 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 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 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 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 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 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 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 96 wells
EUR 629.64

Human VEGFR-3/FLT-4/Fc Chimera, soluble Recombinant Protein

SFC-009 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 100ul
EUR 275
Description: Available in various conjugation types.

Mouse VEGFR-2/Flk-1 (native), soluble Recombinant Protein

S01-M03 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 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 100ul
EUR 429

KDR / VEGFR-2 Antibody

48311-100ul 100ul
EUR 399.6

KDR / VEGFR-2 Antibody

48311-50ul 50ul
EUR 286.8

Human soluble vascular endothelial growth factor receptor-2(VEGFR-2/sFLK-1) Elisa Kit

EK711423 96 Wells
EUR 0.17

Human soluble vascular endothelial growth factor receptor-2,VEGFR-2/sFLK-1 ELISA Kit

CN-03788H1 96T
EUR 576

Human soluble vascular endothelial growth factor receptor-2,VEGFR-2/sFLK-1 ELISA Kit

CN-03788H2 48T
EUR 397.2

Human soluble vascular endothelial growth factor receptor-2(VEGFR-2/sFLK-1) ELISA Kit

NSL0270Hu 96 wells
EUR 468
  • Sandwich ELISA

Human soluble vascular endothelial growth factor receptor-2,VEGFR-2/sFLK-1 ELISA Kit

SL1627Hu 96 Tests
EUR 468
  • 2-8°C

Anti-Human VEGFR-2/KDR-FITC Antibody

101-M20-FITC 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 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 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 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 96 Wells
EUR 0.47

Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit

EKF57716-48T 48T
EUR 396.9

Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit

EKF57716-5x96T 5x96T
EUR 2693.25

Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit

EKF57716-96T 96T
EUR 567

Human SMRP (Soluble Mesothelin Related Peptide) ELISA Kit

EKE61404-5x96T 5x96T
EUR 3124.08

Human SMRP (Soluble Mesothelin Related Peptide) ELISA Kit

EKE61404-96T 96T
EUR 657.7

Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit

EH3796 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 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
  • 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 96 tests
EUR 848.4
  • Shipped within 5-12 working days.

Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit

RE2600H-48wells 48 wells
EUR 116.55
  • Research Area: Enzyme & Kinase

Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit

RE2600H-96wells 96 wells
EUR 161.55
  • Research Area: Enzyme & Kinase

Human Soluble Mesothelin Related Peptide, SMRP ELISA Kit

SELI-66010h 96 Tests
EUR 788.4

Human Soluble Mesothelin Related Peptide,SMRP ELISA Kit

YLA0424HU-48T 48T Ask for price

Human Soluble Mesothelin Related Peptide,SMRP ELISA Kit

YLA0424HU-96T 96T Ask for price

Human FLT-4/VEGFR-3 control/blocking peptide #2

FLT42-P 100 ug
EUR 196.8

Human Soluble Vascular endothelial cell growth factor receptor 1 (VEGFR-1) ELISA Kit

EK5866 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 48 Tests
EUR 290
  • Range: 78.1-5000 pg/mL
Description: Human (Homo sapiens)

Human Soluble Vascular endothelial cell growth factor receptor 1 (VEGFR-1) ELISA Kit

AE11708HU-96Tests 96 Tests
EUR 540
  • Range: 78.1-5000 pg/mL
Description: Human (Homo sapiens)

Anti-Mouse VEGFR-2/KDR, Agonistic Antibody

mV1001r-m 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 1 x 96 wells
EUR 286

Anti-Mouse VEGFR-2/KDR, Antagonistic Antibody

mV1001.1r-m 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 100ul
EUR 476.4

ELISA kit for Human SMRP (Soluble Mesothelin Related Peptide)

E-EL-H5488 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

Anti-Inflammatory Peptide 2

004-02 200 μg
EUR 27

Mouse VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein

SFC-M05 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 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 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 48 Tests
EUR 360
  • Range: 1.56-100 ng/mL
Description: Pig (Sus scrofa; Porcine)

Pig Soluble vascular endothelial growth factor receptor-2 (VEGFR-2/sFLK-1) ELISA Kit

AE63268PI-96Tests 96 Tests
EUR 680
  • Range: 1.56-100 ng/mL
Description: Pig (Sus scrofa; Porcine)

Mouse Soluble Vascular Endothelial Growth Factor Receptor 2(VEGFR-2/sFLK-1)ELISA kit

GA-E0616MS-48T 48T
EUR 403.2

Mouse Soluble Vascular Endothelial Growth Factor Receptor 2(VEGFR-2/sFLK-1)ELISA kit

GA-E0616MS-96T 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 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 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 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 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 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 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 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 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 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 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 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

007-58 100 μg
EUR 158.76

VEGFR binding peptide IVLS / RKRKRKKSRYIVLS

007-59 100 μg
EUR 171.72

VEGFR-KDR/Flk-1 Antagonist Peptide

H-5896.0001 1.0mg
EUR 691.2
Description: Sum Formula: C77H99N23O18S; CAS# [492444-99-2] net

VEGFR-KDR/Flk-1 Antagonist Peptide

H-5896.0005 5.0mg
EUR 2648.4
Description: Sum Formula: C77H99N23O18S; CAS# [492444-99-2] net

Human VEGFR-3/FLT-4, soluble Recombinant Protein

S01-017 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 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 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 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 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 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 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 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 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 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 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 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 96 wells
EUR 629.64

Human VEGFR-3/FLT-4/Fc Chimera, soluble Recombinant Protein

SFC-009 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 100ul
EUR 275
Description: Available in various conjugation types.

Mouse VEGFR-2/Flk-1 (native), soluble Recombinant Protein

S01-M03 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 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 100ul
EUR 429

KDR / VEGFR-2 Antibody

48311-100ul 100ul
EUR 399.6

KDR / VEGFR-2 Antibody

48311-50ul 50ul
EUR 286.8

Human soluble vascular endothelial growth factor receptor-2(VEGFR-2/sFLK-1) Elisa Kit

EK711423 96 Wells
EUR 0.17

Human soluble vascular endothelial growth factor receptor-2,VEGFR-2/sFLK-1 ELISA Kit

CN-03788H1 96T
EUR 576

Human soluble vascular endothelial growth factor receptor-2,VEGFR-2/sFLK-1 ELISA Kit

CN-03788H2 48T
EUR 397.2

Human soluble vascular endothelial growth factor receptor-2(VEGFR-2/sFLK-1) ELISA Kit

NSL0270Hu 96 wells
EUR 468
  • Sandwich ELISA

Human soluble vascular endothelial growth factor receptor-2,VEGFR-2/sFLK-1 ELISA Kit

SL1627Hu 96 Tests
EUR 468
  • 2-8°C

Anti-Human VEGFR-2/KDR-FITC Antibody

101-M20-FITC 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 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 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 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 96 Wells
EUR 0.47

Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit

EKF57716-48T 48T
EUR 396.9

Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit

EKF57716-5x96T 5x96T
EUR 2693.25

Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit

EKF57716-96T 96T
EUR 567

Human SMRP (Soluble Mesothelin Related Peptide) ELISA Kit

EKE61404-5x96T 5x96T
EUR 3124.08

Human SMRP (Soluble Mesothelin Related Peptide) ELISA Kit

EKE61404-96T 96T
EUR 657.7

Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit

EH3796 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 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
  • 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 96 tests
EUR 848.4
  • Shipped within 5-12 working days.

Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit

RE2600H-48wells 48 wells
EUR 116.55
  • Research Area: Enzyme & Kinase

Human SMRP(Soluble Mesothelin Related Peptide) ELISA Kit

RE2600H-96wells 96 wells
EUR 161.55
  • Research Area: Enzyme & Kinase

Human Soluble Mesothelin Related Peptide, SMRP ELISA Kit

SELI-66010h 96 Tests
EUR 788.4

Human Soluble Mesothelin Related Peptide,SMRP ELISA Kit

YLA0424HU-48T 48T Ask for price

Human Soluble Mesothelin Related Peptide,SMRP ELISA Kit

YLA0424HU-96T 96T Ask for price

Human FLT-4/VEGFR-3 control/blocking peptide #2

FLT42-P 100 ug
EUR 196.8

Human Soluble Vascular endothelial cell growth factor receptor 1 (VEGFR-1) ELISA Kit

EK5866 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 48 Tests
EUR 290
  • Range: 78.1-5000 pg/mL
Description: Human (Homo sapiens)

Human Soluble Vascular endothelial cell growth factor receptor 1 (VEGFR-1) ELISA Kit

AE11708HU-96Tests 96 Tests
EUR 540
  • Range: 78.1-5000 pg/mL
Description: Human (Homo sapiens)

Anti-Mouse VEGFR-2/KDR, Agonistic Antibody

mV1001r-m 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 1 x 96 wells
EUR 286

Anti-Mouse VEGFR-2/KDR, Antagonistic Antibody

mV1001.1r-m 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 100ul
EUR 476.4

ELISA kit for Human SMRP (Soluble Mesothelin Related Peptide)

E-EL-H5488 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

Anti-Inflammatory Peptide 2

004-02 200 μg
EUR 27

Mouse VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein

SFC-M05 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 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 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 48 Tests
EUR 360
  • Range: 1.56-100 ng/mL
Description: Pig (Sus scrofa; Porcine)

Pig Soluble vascular endothelial growth factor receptor-2 (VEGFR-2/sFLK-1) ELISA Kit

AE63268PI-96Tests 96 Tests
EUR 680
  • Range: 1.56-100 ng/mL
Description: Pig (Sus scrofa; Porcine)

Mouse Soluble Vascular Endothelial Growth Factor Receptor 2(VEGFR-2/sFLK-1)ELISA kit

GA-E0616MS-48T 48T
EUR 403.2

Mouse Soluble Vascular Endothelial Growth Factor Receptor 2(VEGFR-2/sFLK-1)ELISA kit

GA-E0616MS-96T 96T
EUR 640.8

Mouse Soluble Vascular Endothelial Growth Factor Receptor 2(VEGFR-2/sFLK-1)ELISA kit

YLA0353MO-48T 48T Ask for price

Mouse Soluble Vascular Endothelial Growth Factor Receptor 2(VEGFR-2/sFLK-1)ELISA kit

YLA0353MO-96T 96T Ask for price

Porcine soluble vascular endothelial growth factor receptor-2,VEGFR-2/sFLK-1 Elisa Kit

EK751085 96 Wells
EUR 0.88

PoFAine soluble vascular endothelial growth factor receptor-2,VEGFR-2/sFLK-1 ELISA Kit

CN-01287P1 96T
EUR 590.4

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