PathScan® Total VEGFR-2 Sandwich ELISA Kit #7340
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- ELISA
Important Ordering Details
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Supporting Data
| REACTIVITY | H |
Application Key:
- ELISA-ELISA
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Description
PathScan® Total VEGFR-2 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of total VEGFR-2 protein. A VEGFR-2 mouse mAb has been coated onto the microwells. After incubation with cell lysates, Both nonphospho- and phospho-VEGFR-2 proteins are captured by the coated antibody. Following extensive washing, a VEGFR-2 rabbit mAb is added to detect the captured VEGFR-2 protein. HRP-linked anti-rabbit antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of total VEGFR-2 protein.
*Antibodies in this kit are custom formulations specific to kit.
*Antibodies in this kit are custom formulations specific to kit.
Protocol
Specificity / Sensitivity
CST's PathScan® Total VEGFR-2 Sandwich ELISA Kit detects endogenous levels of total VEGFR-2 protein. Using PathScan® Phospho-VEGFR-2 (Tyr1175) Sandwich ELISA Kit #7335, a significant induction of phospho-VEGFR-2 in HUVEC cells treated with VEGF can be detected. However, the level of total VEGFR-2 (phospho and non-phospho), detected by this Sandwich ELISA Kit #7340, remains unchanged (Figure 1). This kit detects proteins from the indicated species, as determined through in-house testing, but may also detect homologous proteins from other species.
Species Reactivity:
Human
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, PI3 kinase, NCK, and the protein tyrosine phosphatases SHP-1 and SHP-2 (3). Phosphorylation at Tyr1212 provides a docking site for GRB2 binding and phospho-Tyr1175 binds the p85 subunit of PI3 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).
- Meyer, M. et al. (1999) EMBO J 18, 363-74.
- Dougher-Vermazen, M. et al. (1994) Biochem Biophys Res Commun 205, 728-38.
- Kroll, J. and Waltenberger, J. (1997) J Biol Chem 272, 32521-7.
- Takahashi, T. et al. (2001) EMBO J 20, 2768-78.
- Holmqvist, K. et al. (2004) J Biol Chem 279, 22267-75.
- Karkkainen, M.J. and Petrova, T.V. (2000) Oncogene 19, 5598-605.
- Rahimi, N. et al. (2000) J Biol Chem 275, 16986-92.
- Claesson-Welsh, L. (2003) Biochem Soc Trans 31, 20-4.
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