VEGFR-2 Antibody

Vascular endothelial growth factor receptor-2 (VEGFR-2/Flk-1/KDR) is the primary receptor for VEGF in endothelial cells. Other VEGFR family members, VEGFR-1 (Flt-1) and VEGFR-3 (Flt-4), can also transduce the intracellular signals of VEGF. However, the role of VEGFR-1 is observed mainly during embryonic angiogenesis and VEGFR-3 signaling may be restricted to specific types of endothelial cells. Major autophosphorylation sites of VEGFR-2 are located in the kinase insert domain (Tyr-951/996) and in the tyrosine kinase catalytic domain (Tyr-1054/1059) . Other sites, Tyr-1175 and Tyr-1212 provide docking sites for downstream signaling molecules. Activation of VEGFR-2 also phosphorylates Tyr-801, leading to PI3-kinase-Akt activation and increases in endothelial nitric oxide synthase activity. Phosphorylation of mutliple sites in VEGFR-2 is required for downstream activation of several signaling pathways that control proliferation, chemotaxis, and sprouting during angiogenesis.

The antibody detects a 180 kDa* band corresponding to VEGFR-2 in western blots of human endothelial cells, and shows strong reactivity toward recombinant human VEGFR-2, but not VEGFR-1 or VEGFR-3. The antibody also works for immunofluorescent staining of VEGFR-2 in HUVEC cells. This sequence has high homology to rat and mouse VEGFR-2, and no significant homology to other VEGFR family members.