Phospho-VEGF Receptor 2 (Tyr996) Antibody detects endogenous VEGFR 2 only when phosphorylated at tyrosine 996. The antibody cross-reacts with tyrosine-phosphorylated PDGF receptor.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr996 of human VEGF receptor 2. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Vascular endothelial growth factor receptor 2 (VEGFR2, KDR, Flk-1) is a major receptor for VEGF-induced signaling in endothelial cells. Upon ligand binding, VEGFR2 undergoes autophosphorylation and becomes activated (1). Major autophosphorylation sites of VEGFR2 are located in the kinase insert domain (Tyr951/996) and in the tyrosine kinase catalytic domain (Tyr1054/1059) (2). Activation of the receptor leads to rapid recruitment of adaptor proteins, including Shc, Grb2, PI-3 kinase, Nck and the protein tyrosine phosphatases SHP-1 and SHP-2 (3). The phosphorylation of Tyr1212 provides a docking site for Grb2 binding and phospho-Tyr1175 binds with the p85 subunit of PI-3 kinase and PLCγ, as well as Shb (1,4,5). Signaling from VEGFR2 is necessary for the execution of VEGF-stimulated proliferation, chemotaxis and sprouting, as well as survival of cultured endothelial cells in vitro and angiogenesis in vivo (6-8).