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. Cayman's 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.

1. Rauniyar, K., Jha, S.K., and Jeltsch, M. Biology of vascular endothelial growth factor C in the morphogenesis of lymphatic vessels. Front. Bioeng. Biotechnol. 6, 7 (2018).

2. Jha, S.K., Rauniyar, K., Karpanen, T., et al. Efficient activation of the lymphangiogenic growth factor VEGF-C requires the C-terminal domain of VEGF-C and the N-terminal domain of CCBE1. Sci. Rep. 7(1), 4916 (2017).

3. Narko, K., Enholm, B., Mäkinen, T., et al. Effect of inflammatory cytokines on the expression of the vascular endothelial growth factor‐C. Int. J. Exp. Path. 80(3), 109-112 (1999).

4. Enholm, B., Paavonen, K., Ristimäki, A., et al. Comparison of VEGF, VEGF-B, VEGF-C and Ang-1 mRNA regulation by serum, growth factors, oncoproteins and hypoxia. Oncogene 14(20), 2475-2283 (1997).

5. Cao, Y., Linden, P., Farnebo, J., et al. Vascular endothelial growth factor C induces angiogenesis in vivo. Proc. Natl. Acad. Sci. USA 95(24), 14389-14394 (1998).

6. Karkkainen, M.J., Haiko, P., Sainio, K., et al. Vascular endothelial growth factor C is required for sprouting of the first lymphatic vessels from embryonic veins. Nat. Immunol. 5(1), 74-80 (2004).

7. Jain, L., Vargo, C.A., Danesi, R., et al. The role of vascular endothelial growth factor SNPs as predictive and prognostic markers for major solid tumors. Mol. Cancer Ther. 8(9), 2496-2508 (2009).