Cell Signaling Technology

Product Pathways - Tyrosine Kinase / Adaptors

VEGF Receptor 2 Control Proteins #2904

Molecular Weight

110 kDa recombinant kinase fragment

Description

Nonphosporylated VEGFR2 Control Proteins: Purified recombinant human VEGFR2 (Val789-Val1356) expressed as a GST fusion protein in insect cells treated with λ phosphatase. Supplied in SDS Sample Buffer. Store at -20ºC.Phosphorylated VEGFR2 Control Proteins: Purified recombinant human VEGFR2 (Val789-Val1356) expressed as a GST fusion protein in insect cells. Supplied in SDS Sample Buffer. Store at -20ºC.

Directions for Use

As controls, we recommend using 15 µl (20 ng) of phosphorylated and nonphosphorylated VEGFR2 control proteins. Boil sample before use.

Western Blotting

Western Blotting

Western blot analysis of recombinant human GST-VEGF Receptor 2 (Val789-Val1356), untreated or λ phosphatase-treated, using Phospho-VEGF Receptor 2 (Tyr1175) Antibody #2478 (upper), VEGF Receptor 2 Antibody #2479 (lower).

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).

  1. Meyer, M. et al. (1999) EMBO J 18, 363-74.
  2. Dougher-Vermazen, M. et al. (1994) Biochem Biophys Res Commun 205, 728-38.
  3. Kroll, J. and Waltenberger, J. (1997) J Biol Chem 272, 32521-7.
  4. Takahashi, T. et al. (2001) EMBO J 20, 2768-78.
  5. Holmqvist, K. et al. (2004) J Biol Chem 279, 22267-75.
  6. Karkkainen, M.J. and Petrova, T.V. (2000) Oncogene 19, 5598-605.
  7. Rahimi, N. et al. (2000) J Biol Chem 275, 16986-92.
  8. Claesson-Welsh, L. (2003) Biochem Soc Trans 31, 20-4.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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