Recombinant Human Hepatocyte Growth Factor

Hepatocyte Growth Factor (HGF), also known as scatter factor or hepatopoietin A, is a pleiotropic cytokine belonging to the plasminogen-related S1 serine protease family. Structurally, HGF contains an N-terminal PAN/APPLE-like domain, four kringle domains, and a C-terminal serine protease-like domain lacking enzymatic activity. Human HGF is synthesized as an inactive 728 amino acid single-chain precursor that is proteolytically cleaved into an active disulfide-linked heterodimer consisting of an ~60 kDa alpha-chain and ~30 kDa beta-chain. Alternative splicing generates multiple isoforms with truncated domain composition. HGF is highly conserved across mammalian species (>90% sequence identity). HGF binds heparan sulfate proteoglycans and signals through the receptor tyrosine kinase c-MET. Activation of the HGF/c-MET pathway regulates cell proliferation, motility, and morphogenesis, and is implicated in tumor development and progression. Functionally, HGF promotes epithelial cell scattering and branching morphogenesis, partly through upregulation of integrin alpha2beta1, a collagen I receptor. It also modulates cell-cell adhesion via induction of nectin-1 ectodomain shedding. In thyroid cells, HGF stimulates proliferation and migration while suppressing differentiation and TSH-dependent iodine uptake. Additionally, HGF enhances migration of cardiac stem cells in damaged myocardium.