Blocking Peptide
Blocking | 1:1000 |
ELISA | 50 ng/well |
Size 50 μg
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.
References
Garcia Blanes, M. et al. (2007) J Biol. Chem. 282(14):10660.
Kiselyov, A. et al. (2007) Expert Opin. Investig. Drugs 16(1):83.
Robinson, C.J. & Stringer, S.E. (2001) J. Cell Sci.114:853.
Meyer, M. et al. (1999) EMBO J. 18:363.
Dougher-Vermazen, M. et al. (1994) Bioch Biophys Res Com. 205:728.
Western blot image of human K-562 cells (lanes 1 & 2) and HUVEC (lanes 3 & 4). The blots was probed with rabbit polyclonal anti-VEGFR-3 (a.a. 1285-1298) in the absence (lanes 1 & 3) or presence of blocking peptide (VX2945) (lanes 2 & 4).
*For more information, see UniProt Accession P35916
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
This kit contains: