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.¹ 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.^2,1 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.¹ 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.^3,4 VEGFR2 expression is increased in the tumor vasculature of patients with a variety of solid tumors, including colorectal, lung, pancreatic, and breast cancer.⁵ Cayman's 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.

WARNING This product is not for human or veterinary use.

1. Koch, S., and Claesson-Welsh, L. Signal transduction by vascular endothelial growth factor receptors. Cold Spring Harb. Perspect. Med. 2(7), a006502 (2012).

2. Park, S.A., Jeon, M.S., Ha, K.-T., et al. Structure and function of vascular endothelial growth factor and its receptor system. BMB Rep. 51(2), 73-78 (2018).

3. Bowler, E., and Oltean, S. Alternative splicing in angiogenesis. Int. J. Mol. Sci. 20(9), 2067 (2019).

4. Stevens, M., and Oltean, S. Modulation of receptor tyrosine kinase activity through alternative splicing of ligands and receptors in the VEGF-A/VEGFR axis. Cells 8(4), 288 (2019).

5. Smith, N.R., Baker, D., James, N.H., et al. Vascular endothelial growth factor receptors VEGFR-2 and VEGFR-3 are localized primarily to the vasculature in human primary solid cancers. Clin. Cancer Res. 16(14), 3548-3561 (2010).