Cayman VEGF-C (human, recombinant)

VEGF-C is a member of the PDGF/VEGF family of growth factors that promotes lymphangiogenesis.¹ VEGF-C exists as a secreted homodimer composed of a central VEGF homology domain that contains the receptor binding region and is flanked by N- and C-terminal propeptides, which are proteolytically cleaved by furin and ADAMTS3 or plasmin to generate the mature, active protein.^2,3 VEGF-C is produced by macrophages, fibroblasts, smooth muscle cells, and tumor cells.³ VEGFC expression is upregulated by stimulation with IL-1β, TNF-α (Item Nos. 32020 | 32069), PDGF, TGF-β, or EGF (Item Nos. 32057 | 32025) and downregulated by dexamethasone (Item No. 11015).^4,3 Binding of VEGF-C to its receptors, VEGFR2 and VEGFR3, which are expressed by endothelial cells, stimulates the migration, proliferation, and survival of endothelial cells and increases vascular permeability.³ VEGF-C induces angiogenesis in chick embryo chorioallantoic membranes and stimulates proliferation and migration of porcine aortic endothelial cells in vitro.⁵ Genome-wide deletion of Vegfc in mice induces embryonic edema and defects in lymphatic vascular development and is perinatal lethal.⁶ Increased VEGF-C tumor levels are positively correlated with poor prognosis, decreased overall survival, and resistance to hormone therapy in patients with breast cancer.⁷ VEGFC SNPs have been found in patients with non-small cell lung cancer (NSCLC), as well as colorectal or prostate cancer. Caymans VEGF-C (human, recombinant) protein can be used for binding and cell-based assay applications. This protein consists of 136 amino acids, has a calculated molecular weight of 15.5 kDa, and a predicted N-terminus of Thr103 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is approximately 22 to 24 kDa due to glycosylation.

WARNING This product is not for human or veterinary use.