Product Name: KDR (1051-1063) pY1054+pY1059
Product Number: PE-04AUI75
Size: 200 µg      Price:20.00
1 mg      $US41.00
Peptide Name: KDR (1051-1063) pY1054+pY1059

Product Use: This phosphopeptide may be useful as a substrate for screening the phosphatase activity of protein phosphatases. The peptide sequence is located in the protein kinase catalytic domain activation T-loop between subdomains VII and VIII. Y1054 and Y1059 phosphorylation stimulate phosphotransferase activity.

Peptide Production Method: Solid-phase peptide synthesis

Peptide Origin: Homo sapiens

Peptide Sequence: RDI-pY-KDPD-pY-VRKG

Peptide Modifications N Terminus: Free amino

Peptide Modifications C Terminus: βAla-Cys

Peptide Modifications Other: Phosphorylated
Peptide Molecular Mass Calculated: 2114.1 Da

Peptide Purity Percent after Synthesis and Purification: >50

Peptide Appearance: White powder

Peptide Form: Solid

Storage Conditions: -20°C

Scientific Background: VEGFR2 (KDR, FLK1) is a protein-tyrosine kinase of the TK group and VEGFR (vascular endothelial growth factor receptor) family. It is a receptor kinase that binds VEGFA, VEGFC, and VEGFD, and has an essential function in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. VEGFR2 activation promotes the proliferation, survival, migration, and differentiation of endothelial cells. It is activated by binding VEGF, which induces dimerization and autophosphorylation at the following phosphosites, which all contribute to increased phosphotransferase activity. In addition, autophosphorylation of Y801 induces interaction with PIK3R1, autophosphorylation of Y951 and Y1008 induces interaction with PLCg1, autophosphorylation of Y1054, Y996 and Y1059 induces interaction with PLCg1, and autophosphorylation of Y1175 induces interaction with PLCg1, Shb, Shc1 and Shc2. KDR mediates the activation of the ERK1/2 MAP kinase intracellular signalling pathways. VEGFR2 appears to be an oncoprotein (OP). Mutations in the VEGFR2 gene have been observed in patients with hemangioma. Significantly higher VEGFR2 expression was observed in metastatic as compared to non-metastatic human colon cancer cell lines, which directly correlated with increased neovascularization and tumour cell proliferation. Elevated VEGFR2 expression was also correlated with blood vessel count in human intestinal-type gastric cancers, and in tumour cells in primary and metastatic ovarian carcinomas. VEGF signalling is vital to the early stages of tumour progression in mouse models of squamous skin tumours. In addition, inhibition of VEGFR2 resulted in tumour regression through decreased microvasculature and impaired ability to maintain the stem-like characteristic of the tumour cells.