Recombinant Human VEGF-C is a disulfide-linked homodimeric protein composed of two 13.5 kDa polypeptide chains, each containing 116 amino acid residues. As a member of the PDGF/VEGF family, VEGF-C plays crucial roles in angiogenesis, endothelial cell growth, and blood vessel permeability. It undergoes complex proteolytic processing, resulting in multiple forms with varying receptor affinities. The various processed forms of VEGF-C can bind and activate VEGFR-3 receptors, while only the fully processed form can bind and activate VEGFR-2 receptors. Structurally and functionally similar to vascular endothelial growth factor D (VEGF-D), VEGF-C stimulates lymphangiogenesis and angiogenesis, promotes endothelial cell proliferation and migration, increases blood vessel permeability, plays a role in embryonic development of venous and lymphatic vascular systems, and maintains differentiated lymphatic endothelium in adults.