BACKGROUND VEGFR1 (Flt-1) and VEGFR2 (KDR/Flk-1) play an important role in regulating physiological as well as pathological angiogenesis. VEGFR2 has strong tyrosine kinase activity, and transduces the major signals for angiogenesis. However, unlike other representative tyrosine kinase receptors which use the Ras pathway, VEGFR2 mostly uses the Phospholipase-C-gamma-Protein kinase-C pathway to activate MAP-kinase and DNA synthesis. VEGFR2 is a direct signal transducer for pathological angiogenesis including cancer and diabetic retinopathy, thus, VEGFR2 itself and the signaling pathway appear to be critical targets for the suppression of these diseases.1,2 Upon binding to its ligand most commonly including VEGF-A and VEGF-E, VEGFR2 undergoes dimerization and becomes activated. Autophosphorylation of tyrosine 1054 in its kinase catalytic domain is required for tyrosine kinase activity.3
1. Olsson, A. K. et al: Nat Rev Mol Cell Biol 7:359-71, 2006.
2. Shibuya, M.: J Biochem Mol Biol. 39:469-78, 2006.
3. Paz, K. & Zhu, Z.: Front Biosci. 10:1415-39, 2005.
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15 amino acid residues surrounding human VEGFR2 phospho-Tyr1054.
Affinity Purified Rabbit IgG
Species & predicted
reactivity ( ):
IHC (Paraffin) n/d
Weight of protein:
This antibody detects endogenous levels of phosphorylated VEGFR2.
Store at 4° C for frequent use; at -20° C for at least one year.
*Optimal working dilutions must be determined by end user.