VEGF-A 165 variant (human, recombinant)

VEGF-A is a member of the PDGF/VEGF family of growth factors that regulates the development, proliferation, and maintenance of the vascular system.¹ VEGF-A exists as a homodimer and is secreted by endothelial cells, as well as fibroblasts, smooth muscle cells, platelets, neutrophils, and macrophages.^2,3 Alternative splicing of VEGFA pre-mRNA leads to the formation of eight isoforms, including the pro-angiogenic VEGF-A 165 variant (VEGF-165), which is the most abundant and biologically active form.^4,5 VEGF-165 is composed of a signal peptide, a VEGFR1-binding domain, a VEGFR2-binding domain, a heparin-binding domain, and a C-terminal domain, which interacts with the extracellular matrix (ECM) and neuropilin (NRP).^4,6 It is involved in embryonic development, wound healing, and neovascularization in diseases such as cancer.⁵ VEGF-165 induces angiogenesis in rabbit cornea, which can be reversed by the anti-angiogenic factor VEGF-165b.⁷ Serum levels of VEGF-165 are increased in patients with melanoma and positively correlated with metastasis.⁸ VEGF-165 levels are also increased in the serum, synovial fluid, and inflamed joints of patients with rheumatoid arthritis.⁹ Cayman’s VEGF-A 165 variant (human, recombinant) protein can be used for binding assay and cell-based assay applications. This protein consists of 165 amino acids and a predicted N-terminus of Ala27 after signal peptide cleavage.

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1. Shibuya, M. Vascular endothelial growth factor (VEGF) and its receptor (VEGFR) signaling in angiogenesis: A crucial target for anti- and pro-angiogenic therapies. Genes Cancer 2(12), 1097-1105 (2011).

2. Guzmán-Hernández, M.L., Potter, G., Egervári, K., et al. Secretion of VEGF-165 has unique characteristics, including shedding from the plasma membrane. Mol. Biol. Cell 25(7), 1061-1072 (2014).

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

4. Peach, C.J., Mignone, V.W., Arruda, M.A., et al. Molecular pharmacology of VEGF-A isoforms: Binding and signalling at VEGFR2. Int. J. Mol. Sci. 19(4), 1264 (2018).

5. Holmes, D.I.R., and Zachary, I. The vascular endothelial growth factor (VEGF) family: Angiogenic factors in health and disease. Genome Biol. 6(2), 209 (2005).

6. Harper, S.J., and Bates, D.O. VEGF-A splicing: The key to anti-angiogenic therapeutics? Nat. Rev. Cancer 8(11), 880-887 (2008).

7. Woolard, J., Wang, W.Y., Bevan, H.S., Qiu, Y., et al. VEGF165b, an inhibitory vascular endothelial growth factor splice variant: Mechanism of action, in vivo effect on angiogenesis and endogenous protein expression. Cancer Res. 64(21), 4822-7835 (2004).

8. Osella-Abate, S., Quaglino, P., Savoia, P., et al. VEGF-165 serum levels and tyrosinase expression in melanoma patients: Correlation with the clinical course. Melanoma Res. 12(4), 325-334 (2002).

9. Yoo, S.-A., Kwok, S.-K., and Kim, W.-U. Proinflammatory role of vascular endothelial growth factor in the pathogenesis of rheumatoid arthritis: Prospects for therapeutic intervention. Mediators Inflamm. 129873 (2008).