VEGF-D, a member of the VEGF/PDGF family of structurally related proteins, is a potent angiogenic cytokine. It promotes endothelial cell growth, promotes lymphangiogesis, and can also affect vascular permeability. VEGF-D is highly expressed in the lung, heart, small intestine and fetal lung, and at lower levels in the skeletal muscle, colon, and pancreas. It forms cell surface-associated, non-covalent, disulfide-linked homodimers, and can bind and activate both VEGFR-2 (flk1) and VEGFR-3 (flt4) receptors. During embryogenesis, VEGF-D may play a role in the formation of the venous and lymphatic vascular systems. It also participates in the growth and maintenance of differentiated lymphatic endothelium in adults. 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-D is a 26.2 kDa, non-disulfide linked, homodimeric protein consisting of two 117 amino acid polypeptide chains. Due to glycosylation, the protein migrates as a 20.0-22.0 kDa band by SDS-PAGE analysis under non-reducing conditions.
Vascular Endothelial Growth Factor-D, FIGF
AA Sequence (monomer):
FAATFYDIET LKVIDEEWQR TQCSPRETCV EVASELGKST NTFFKPPCVN VFRCGGCCNE ESLICMNTST SYISKQLFEI SVPLTSVPEL VPVKVANHTG CKCLPTAPRH PYSIIRR
≥ 95% by SDS-PAGE gel and HPLC analyses.
Measured by its ability to bind immobilized recombinant
human Neuropilin-1 in an ELISA.