HGF Recombinant Rabbit Monoclonal Antibody [PSH03-79]

Function

HGF, also known as scatter factor and hepatopoietin A, is a pleiotropic protein in the plasminogen subfamily of S1 peptidases. It is a multidomain molecule that includes an N-terminal PAN/APPLE-like domain, four Kringle domains, and a serine proteinase-like domain that has no detectable protease activity Human HGF is secreted as an inactive 728 amino acid (aa) single chain propeptide. It is cleaved after the fourth Kringle domain by a serine protease to form bioactive disulfide-linked HGF with a 60 kDa alpha and 30 kDa beta chain. Alternate splicing generates human HGF isoforms that lack the proteinase-like domain and different numbers of the Kringle domains. Human HGF shares 91%-94% aa sequence identity with bovine, canine, feline, mouse, and rat HGF. HGF binds heparan-sulfate proteoglycans and the widely expressed receptor tyrosine kinase, HGF R/c-MET. HGF-dependent c-MET activation is implicated in the development of many human cancers. HGF regulates epithelial morp.

Background References

1. Stamos J., Lazarus R.A., Yao X., Kirchhofer D., Wiesmann C. Crystal structure of the HGF beta-chain in complex with the Sema domain of the Met receptor. EMBO J. 23:2325-2335 (2004)

2. Tolbert W.D., Daugherty-Holtrop J., Gherardi E., Vande Woude G., Xu H.E. Structural basis for agonism and antagonism of hepatocyte growth factor. Proc. Natl. Acad. Sci. U.S.A. 107:13264-13269 (2010)

Subcellular Location

Extracellular region, Extracellular space.

UNIPROT

SwissProt: P14210 Human

Synonyms