Cayman VEGFR2 Extracellular Domain (human, recombinant; aa 20-327)

VEGFR2, also known as kinase insert domain receptor (KDR), is a receptor tyrosine kinase that has roles in vascular permeability, cell proliferation and survival, and angiogenesis. It is composed of an N-terminal extracellular ligand-binding domain, which contains seven immunoglobulin-like (Ig-like) domains, a transmembrane domain, and an intracellular tyrosine kinase domain, which is subject to phosphorylation and contains a kinase insert domain and the C-terminal domain.^, VEGFR2 is expressed primarily in vascular and lymphatic endothelial cells, where it is bound by the growth factors VEGF-A, VEGF-C, and VEGF-D. Upon ligand binding, VEGFR2 forms homodimers or heterodimers with VEGFR1 or VEGFR3, resulting in VEGFR2 phosphorylation and activation of a variety of intracellular signaling pathways, including the ERK/MAPK pathway, to promote endothelial cell survival, proliferation, and migration. VEGFR2 also exists in a soluble form that is generated by alternative splicing of the KDR pre-mRNA or proteolytic shedding and decreases angiogenesis by functioning as a decoy receptor for VEGF-A.^, VEGFR2 expression is increased in the tumor vasculature of patients with a variety of solid tumors, including colorectal, lung, pancreatic, and breast cancer. Caymans VEGFR2 Extracellular Domain (human, recombinant; aa 20-327) protein can be used for enzyme activity assays. This protein is a disulfide-linked homodimer. The reduced monomer, comprised of VEGFR2 (amino acids 20-327) fused to human IgG1 Fc at its C-terminus, consists of 549 amino acids, has a calculated molecular weight of 61.5 kDa, and a predicted N terminus of Ala20 after signal peptide cleavage. As a result of glycosylation, the monomer migrates at greater than 61.5 kDa by SDS-PAGE under reducing conditions.

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