Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to inhibit the VEGF-dependent proliferation of HUVEC human umbilical vein endothelial cells. The ED50 for this effect is 10-40 ng/mL in the presence of 10 ng/mL recombinant human VEGF165. |
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Source | Mouse myeloma cell line, NS0-derived human VEGFR2/KDR/Flk-1 protein
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Accession # | |||||||||
N-terminal Sequence | Ala20 |
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Structure / Form | Disulfide-linked homodimer |
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Protein/Peptide Type | Recombinant Proteins |
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Gene | KDR |
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Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 110 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 160-170 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
VEGFR2 (KDR/Flk-1), VEGFR1 (Flt-1) and VEGFR3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domains and kinase insert domains in their intracellular regions. The expression of VEGFR1, 2, and 3 is almost exclusively restricted to the endothelial cells. These receptors are likely to play essential roles in vasculogenesis and angiogenesis.
VEGFR2 cDNA encodes a 1356 amino acid (aa) residue precursor protein with a 19 aa residue signal peptide. Mature VEGFR2 is composed of a 745 aa residue extracellular domain, a 25 aa residue transmembrane domain and a 567 aa residue cytoplasmic domain. In contrast to VEGFR1 which binds both PlGF and VEGF with high affinity, VEGFR2 binds VEGF but not PlGF with high affinity. The recombinant soluble VEGFR2/Fc chimera binds VEGF with high affinity and is a potent VEGF antagonist.
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