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.

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.

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.

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.)

Human VEGFR-2/KDR (D7), soluble
MBS691482-005mg	MyBiosource	0.05mg	EUR 415

Human VEGFR-2/KDR (D7), soluble
MBS691482-5x005mg	MyBiosource	5x0.05mg	EUR 1575

Human VEGFR-2/KDR (D7), soluble
MBS692026-0005mg	MyBiosource	0.005mg	EUR 220

Human VEGFR-2/KDR (D7), soluble
MBS692026-5x0005mg	MyBiosource	5x0.005mg	EUR 695

Human VEGFR-2/KDR (native), soluble
MBS691515-0005mg	MyBiosource	0.005mg	EUR 340

Human VEGFR-2/KDR (native), soluble
MBS691515-5x0005mg	MyBiosource	5x0.005mg	EUR 1245

Human VEGFR-2/KDR (native), soluble
MBS691865-002mg	MyBiosource	0.02mg	EUR 565

Human VEGFR-2/KDR (native), soluble
MBS691865-5x002mg	MyBiosource	5x0.02mg	EUR 2245

Human VEGFR-2/KDR-Fc Chimera, soluble
MBS691815-005mg	MyBiosource	0.05mg	EUR 395

Human VEGFR-2/KDR-Fc Chimera, soluble
MBS691815-5x005mg	MyBiosource	5x0.05mg	EUR 1490

Human VEGFR-2/KDR-Fc Chimera, soluble
MBS692025-001mg	MyBiosource	0.01mg	EUR 245

Human VEGFR-2/KDR-Fc Chimera, soluble
MBS692025-5x001mg	MyBiosource	5x0.01mg	EUR 805

Rabbit Anti-Mouse VEGFR-2 Flk-1 (Peptide), soluble
103-PA19	Angio Proteomie	100ug	EUR 240

Anti-Mouse VEGFR-2/Flk-1 (Peptide), soluble Antibody
103-PA19S	ReliaTech	100 µg	EUR 126
Description: The antibody recognizes solely the endogenous soluble form of mouse vascular endothelial growth factor receptor 2, alos known as CD309, VEGFR2, KDR, protein tyrosine kinase receptor flk-1, and fetal liver kinase-1. The endogenous soluble mouse esFlk-1 generated by alternative splicing consists of the first 6 Ig-like loops followed by the unique C-terminal end: GMEASLGDRIAMP. Flk-1 is a member of the tyrosine protein kinase family, sub-family CSF-1/PDGF, that contains a single pass transmembrane receptor with a protein kinase domain and seven immunoglobulin-like domains in the extracellular region. Flk-1 is expressed at high levels in adult heart, lung, kidney, brain, and skeletal muscle; other tissues express at lower levels. Flk-1 is a receptor for VEGF-A or fully processed VEGF-C; ligand binding plays a key role in vascular development and vascular permeability.

Rabbit Anti-Human VEGFR-1 Flt-1 (Peptide), soluble
102-PA21	Angio Proteomie	100ug	EUR 240

Anti-Human VEGFR-1/Flt-1 (Peptide), soluble Antibody
102-PA21S	ReliaTech	100 µg	EUR 126
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA.

Human VEGFR-2/KDR (D7), soluble Recombinant Protein
S01-001	ReliaTech	5 µg	EUR 42
Description: Recombinant Human soluble Endothelial Growth Factor Receptor-2 (sKDR(D7)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein consists of all 7 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 116 kDa.Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Human VEGFR-2/KDR (D7), soluble Recombinant Protein
S01-002	ReliaTech	50 µg	EUR 183.75
Description: Recombinant Human soluble Endothelial Growth Factor Receptor-2 (sKDR(D7)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein consists of all 7 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 116 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Human VEGFR-2/KDR (native), soluble Recombinant Protein
S01-003	ReliaTech	5 µg	EUR 126
Description: The naturally occuring form of human soluble Endothelial Growth Factor Receptor-2 (sKDR) was cloned from a full length KDR cDNA by standard molecular methods. The soluble receptor protein consists of the first 6 extracellular domains and contains the unique C-terminal end of native human soluble VEGFR-2/KDR (CGRETILDHSAEAVGMP) generated by alternative splicing. The recombinant human sKDR is produced in a monomeric form in insect cells. The receptor monomers have a mass of approximately 105 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). For Flt-1 as well as KDR naturally occuring soluble forms are described. The expression of the receptors is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Human VEGFR-2/KDR (native), soluble Recombinant Protein
S01-004	ReliaTech	20 µg	EUR 273
Description: The naturally occuring form of human soluble Endothelial Growth Factor Receptor-2 (sKDR) was cloned from a full length KDR cDNA by standard molecular methods. The soluble receptor protein consists of the first 6 extracellular domains and contains the unique C-terminal end of native human solubleVEGFR-2/KDR (CGRETILDHSAEAVGMP) generated by alternative splicing. The recombinant human sKDR is produced in a monomeric form in insect cells. The receptor monomers have a mass of approximately 105 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). For Flt-1 as well as KDR naturally occuring soluble forms are described. The expression of the receptors is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Anti-Human VEGFR1-14/Flt1-14 (peptide), soluble Antibody
101-M29	ReliaTech	100 µg	EUR 199.5
Description: A human-specific splicing variant of vascular endothelial growth factor (VEGF) receptor 1 (Flt1) was discovered, producing a soluble receptor (designated sFlt1-14) that is qualitatively different from the previously described soluble receptor (sFlt1) and functioning as a potent VEGF inhibitor. sFlt1-14 is generated in a cell type-specific fashion, primarily in non-endothelial cells. Notably, in vascular smooth muscle cells, all Flt1 messenger RNA is converted to sFlt1-14, whereas endothelial cells of the same human vessel express sFlt1. sFlt1-14 expression by vascular smooth muscle cells is dynamically regulated as evidenced by its upregulation on coculture with endothelial cells or by direct exposure to VEGF. Increased production of soluble VEGF receptors during pregnancy is entirely attributable to induced expression of placental sFlt1-14 starting by the end of the first trimester. Expression is dramatically elevated in the placenta of women with preeclampsia, specifically induced in abnormal clusters of degenerative syncytiotrophoblasts known as syncytial knots, where it may undergo further messenger RNA editing. sFlt1-14 is the predominant VEGF-inhibiting protein produced by the preeclamptic placenta, accumulates in the circulation, and hence is capable of neutralizing VEGF in distant organs affected in preeclampsia. Together, these findings revealed a new natural VEGF inhibitor that has evolved in humans, possibly to protect non-endothelial cells from adverse VEGF signaling. Furthermore, the study uncovered the identity of a VEGF-blocking protein implicated in preeclampsia.

VEGFR binding peptide KH / QKRKRKKSRKKH
007-58	PHOENIX PEPTIDE	100 μg	EUR 158.76

VEGFR binding peptide IVLS / RKRKRKKSRYIVLS
007-59	PHOENIX PEPTIDE	100 μg	EUR 171.72

Human VEGFR-1 ELISA (soluble)
MBS691466-0096mg	MyBiosource	0.096mg	EUR 815

Human VEGFR-1 ELISA (soluble)
MBS691466-5x0096mg	MyBiosource	5x0.096mg	EUR 3625

Human VEGFR-3/FLT-4, soluble
MBS691602-001mg	MyBiosource	0.01mg	EUR 310

Human VEGFR-3/FLT-4, soluble
MBS691602-5x001mg	MyBiosource	5x0.01mg	EUR 1110

Human VEGFR-3/FLT-4, soluble
MBS691970-005mg	MyBiosource	0.05mg	EUR 465

Human VEGFR-3/FLT-4, soluble
MBS691970-5x005mg	MyBiosource	5x0.05mg	EUR 1805

Human VEGFR-3/FLT-4, soluble
MBS692181-0005mg	MyBiosource	0.005mg	EUR 250

Human VEGFR-3/FLT-4, soluble
MBS692181-5x0005mg	MyBiosource	5x0.005mg	EUR 835

Human VEGFR-1/Flt1-14, soluble
MBS692285-0005mg	MyBiosource	0.005mg	EUR 340

Human VEGFR-1/Flt1-14, soluble
MBS692285-002mg	MyBiosource	0.02mg	EUR 530

Human VEGFR-1/Flt1-14, soluble
MBS692285-5x002mg	MyBiosource	5x0.02mg	EUR 2085

Human VEGFR-1/Flt-1 (D5), soluble
MBS691664-002mg	MyBiosource	0.02mg	EUR 380

Human VEGFR-1/Flt-1 (D5), soluble
MBS691664-5x002mg	MyBiosource	5x0.02mg	EUR 1410

Human VEGFR-1/Flt-1 (D5), soluble
MBS691669-0005mg	MyBiosource	0.005mg	EUR 265

Human VEGFR-1/Flt-1 (D5), soluble
MBS691669-5x0005mg	MyBiosource	5x0.005mg	EUR 890

Human VEGFR-1/Flt-1 (D3), soluble
MBS691717-002mg	MyBiosource	0.02mg	EUR 450

Human VEGFR-1/Flt-1 (D3), soluble
MBS691717-5x002mg	MyBiosource	5x0.02mg	EUR 1725

Human VEGFR-1/Flt-1 (D4), soluble
MBS691847-0005mg	MyBiosource	0.005mg	EUR 310

Human VEGFR-1/Flt-1 (D4), soluble
MBS691847-5x0005mg	MyBiosource	5x0.005mg	EUR 1110

Human VEGFR-1/Flt-1 (D3), soluble
MBS692000-0005mg	MyBiosource	0.005mg	EUR 310

Human VEGFR-1/Flt-1 (D3), soluble
MBS692000-5x0005mg	MyBiosource	5x0.005mg	EUR 1110

Human VEGFR-1/Flt-1 (D4), soluble
MBS692119-002mg	MyBiosource	0.02mg	EUR 450

Human VEGFR-1/Flt-1 (D4), soluble
MBS692119-5x002mg	MyBiosource	5x0.02mg	EUR 1725

Human VEGFR-1/Flt-1 (native), soluble
MBS691505-0005mg	MyBiosource	0.005mg	EUR 265

Human VEGFR-1/Flt-1 (native), soluble
MBS691505-5x0005mg	MyBiosource	5x0.005mg	EUR 890

Human VEGFR-1/Flt-1 (native), soluble
MBS691991-002mg	MyBiosource	0.02mg	EUR 380

Human VEGFR-1/Flt-1 (native), soluble
MBS691991-5x002mg	MyBiosource	5x0.02mg	EUR 1410

Rabbit Anti-Mouse VEGFR-2 Flk-1, soluble
103-PA18	Angio Proteomie	100ug	EUR 240

Human VEGFR-1/Flt-1 (D3)-His, soluble
MBS692528-005mg	MyBiosource	0.05mg	EUR 725

Human VEGFR-1/Flt-1 (D3)-His, soluble
MBS692528-5x005mg	MyBiosource	5x0.05mg	EUR 2965

Human VEGFR-3/FLT-4/Fc Chimera, soluble
MBS691672-005mg	MyBiosource	0.05mg	EUR 430

Human VEGFR-3/FLT-4/Fc Chimera, soluble
MBS691672-5x005mg	MyBiosource	5x0.05mg	EUR 1645

Human VEGFR-3/FLT-4/Fc Chimera, soluble
MBS691800-001mg	MyBiosource	0.01mg	EUR 265

Human VEGFR-3/FLT-4/Fc Chimera, soluble
MBS691800-5x001mg	MyBiosource	5x0.01mg	EUR 890

Human VEGFR-3/FLT-4/Fc Chimera, soluble
SFC-010	Angio Proteomie	50ug	EUR 378

Rabbit anti VEGFR-2/KDR (human)
102-PA18AG	Angio Proteomie	50ug	EUR 240

Rabbit anti VEGFR-2/KDR (human)
102-PA18S	Angio Proteomie	100ug	EUR 240

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691483-005mg	MyBiosource	0.05mg	EUR 395

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691483-5x005mg	MyBiosource	5x0.05mg	EUR 1490

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691782-001mg	MyBiosource	0.01mg	EUR 245

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691782-5x001mg	MyBiosource	5x0.01mg	EUR 805

Human VEGFR-3/FLT-4, soluble Recombinant Protein
S01-017	ReliaTech	10 µg	EUR 103.95
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.

Human VEGFR-3/FLT-4, soluble Recombinant Protein
S01-017S	ReliaTech	5 µg	EUR 63
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.

Human VEGFR-3/FLT-4, soluble Recombinant Protein
S01-018	ReliaTech	50 µg	EUR 210
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23 aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751 aa residue extracellular domain, a 22 aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.

VEGFR-KDR/Flk-1 Antagonist Peptide
H-5896.0001	Bachem	1.0mg	EUR 691.2
Description: Sum Formula: C77H99N23O18S; CAS# [492444-99-2] net

VEGFR-KDR/Flk-1 Antagonist Peptide
H-5896.0005	Bachem	5.0mg	EUR 2648.4
Description: Sum Formula: C77H99N23O18S; CAS# [492444-99-2] net

Mouse VEGFR-2/Flk-1 (native), soluble
MBS691679-0005mg	MyBiosource	0.005mg	EUR 340

Mouse VEGFR-2/Flk-1 (native), soluble
MBS691679-5x0005mg	MyBiosource	5x0.005mg	EUR 1245

Mouse VEGFR-2/Flk-1 (native), soluble
MBS691714-002mg	MyBiosource	0.02mg	EUR 565

Mouse VEGFR-2/Flk-1 (native), soluble
MBS691714-5x002mg	MyBiosource	5x0.02mg	EUR 2245

Mouse anti VEGFR-2/KDR (#3) (human)
101-M32	Angio Proteomie	100ug	EUR 297.6

Mouse anti VEGFR-2/KDR (#4) (human)
101-M34	Angio Proteomie	100ug	EUR 297.6

Mouse anti VEGFR-2/KDR (#EIC) (human)
101-M20	Angio Proteomie	100ug	EUR 297.6

Mouse anti VEGFR-2/KDR (#EWC) (human)
101-M22	Angio Proteomie	100ug	EUR 297.6

Human VEGFR-1/Flt-1 (D5), soluble Recombinant Protein
S01-011	ReliaTech	5 µg	EUR 73.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-5 (sVEGFR-1(D5)) is a 70 kDa protein. The baculovirus generated, recombinant human sVEGFR-1 is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 70 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D5), soluble Recombinant Protein
S01-012	ReliaTech	20 µg	EUR 157.5
Description: Recombinat human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-5 (sVEGFR-1(D5)) is a 70 kDa protein containing amino acid residues. The baculovirus generated, recombinant human sVEGFR-1 is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 70 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D4), soluble Recombinant Protein
S01-013	ReliaTech	5 µg	EUR 103.95
Description: Recombinant Human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-4 (sVEGFR-1(D4)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 4 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 55 kDa containing 457 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D4), soluble Recombinant Protein
S01-014	ReliaTech	20 µg	EUR 199.5
Description: Recombinant Human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-4 (sVEGFR-1(D4)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 4 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 55 kDa containing 457 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D3), soluble Recombinant Protein
S01-015	ReliaTech	5 µg	EUR 103.95
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D3), soluble Recombinant Protein
S01-016	ReliaTech	20 µg	EUR 199.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Rabbit anti VEGFR-2/KDR-Biotin (human)
102-PABi18	Angio Proteomie	50ug	EUR 297.6

Human VEGFR-1/Flt-1 (native), soluble Recombinant Protein
S01-009	ReliaTech	5 µg	EUR 73.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1) is the naturally occurring form and was cloned from total RNA of human umbilical vein endothelial cells. The recombinant mature sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96 kDa. The soluble receptor precursor protein consists of the first 6 extracellular domains (Met1-His688) containing the unique 31 amino acids residues at the C-terminus. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly, a naturally occurring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (native), soluble Recombinant Protein
S01-010	ReliaTech	20 µg	EUR 157.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1) is the naturally occurring form and was cloned from total RNA of human umbilical vein endothelial cells. The recombinant mature sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96 kDa. The soluble receptor protein consists of the first 6 extracellular domains (Met1-His688) containing the unique 31 amino acids residues at the C-terminus. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly, a naturally occurring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D3)-His, soluble Recombinant Protein
S01-080	ReliaTech	50 µg	EUR 378
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Soluble ST2 (Human) - ELISA Kit
EK-036-10	PHOENIX PEPTIDE	96 wells	EUR 629.64

Human VEGFR-3/FLT-4/Fc Chimera, soluble Recombinant Protein
SFC-009	ReliaTech	10 µg	EUR 73.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-3/Fc is a disulfide-linked homodimeric protein. The sVEGFR-3/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The VEGFR-3/FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The FLT-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial at latter stages of development. It is important for lymphangiogenesis.

Mouse Anti-Human VEGFR-2/KDR
MBS690191-01mg	MyBiosource	0.1mg	EUR 450

Mouse Anti-Human VEGFR-2/KDR
MBS690191-5x01mg	MyBiosource	5x0.1mg	EUR 1725

Mouse Anti-Human VEGFR-2/KDR
MBS690287-01mg	MyBiosource	0.1mg	EUR 430

Mouse Anti-Human VEGFR-2/KDR
MBS690287-5x01mg	MyBiosource	5x0.1mg	EUR 1645

Mouse Anti-Human VEGFR-2/KDR
MBS690550-01mg	MyBiosource	0.1mg	EUR 430

Mouse Anti-Human VEGFR-2/KDR
MBS690550-5x01mg	MyBiosource	5x0.1mg	EUR 1645

Mouse Anti-Human VEGFR-2/KDR
MBS690551-005mg	MyBiosource	0.05mg	EUR 450

Mouse Anti-Human VEGFR-2/KDR
MBS690551-5x005mg	MyBiosource	5x0.05mg	EUR 1725