Human VEGF-165 Recombinant Protein

VEGF-165 is the most abundant splice variant of VEGF-A (1,2). VEGF-165 is produced by a number of cells including endothelial cells, macrophages, and T cells. VEGF-165 is involved in angiogenesis, vascular endothelial cell survival, growth, migration, and vascular permeability (1). VEGF gene expression is induced by hypoxia, inflammatory cytokines, and oncogenes (1,2). VEGF-165 binds to heparan sulfate and is retained on the cell surface and in the extracellular matrix (2,3). VEGF-165 binds to the receptor tyrosine kinases, VEGFR1 and VEGFR2 (1). VEGF-165 is the only splice variant that binds to co-receptors NRP-1 and NRP-2 (1-3) that function to enhance VEGFR2 signaling (1). Binding of VEGF-165 to VEGFR1 and VEGFR2 leads to activation of PI3K/Akt, p38 MAPK, FAK and paxillin (1). VEGF plays a key role in tumor angiogenesis in many cancers (2).

Endotoxin levels are less than or equal to 1 EU / 1 μg hVEGF-165.

A greater than or equal to 95% purity was determined by SDS-PAGE.

Recombinant human VEGF-165 was expressed in E. coli and is supplied in a lyophilized form.

The bioactivity of recombinant hVEGF-165 was determined in a HUVEC cell proliferation assay. The ED₅₀ of each lot is less than or equal to 10 ng/ml.