VEGF-C, a member of the VEGF/PDGF family of structurally-related proteins, is a potent angiogenic cytokine. It promotes endothelial cell growth, promotes lymphangiogenesis, and can also affect vascular permeability. VEGF-C is expressed in various tissues, but is not produced in peripheral blood lymphocytes. It forms cell surfaced-associated, non-covalent, disulfide-linked homodimers, and can bind and activate both VEGFR-2 (flk1) and VEGFR-3 (flt4) receptors. During embryogenesis, VEGF-C may play a role in the formation of the venous and lymphatic vascular systems. Both VEGF-C and VEGF-D are over-expressed in certain cancers, and the resulting elevated levels of VEGF-C or VEGF-D tend to correlate with increased lymphatic metastasis. Recombinant Human VEGF-C is a non-disulfide-linked homodimeric protein consisting of two 13.5 kDa polypeptide chains of 116 amino acid residues. Due to glycosylation, the protein migrates as a 20.0-22.0 kDa band by SDS-PAGE analysis under non-reducing conditions.