Recombinant Human HGF (C-6His)

Hepatocyte Growth Factor (HGF) is a pleiotropic protein belonging to the plasminogen-related subfamily of S1 peptidases. It contains four kringle domains, one PAN domain, and one peptidase S1 domain. HGF is initially synthesized and secreted as a 728 amino acid single-chain precursor (pro-HGF), which undergoes proteolytic cleavage by a serine protease after the fourth kringle domain. This cleavage yields the bioactive, disulfide-linked heterodimeric form consisting of a 60 kDa alpha-chain and a 30 kDa beta-chain. HGF binds to heparan sulfate proteoglycans and exerts its biological functions through interaction with the receptor tyrosine kinase c-MET. Ligand binding to c-MET triggers a cascade of downstream signaling events that regulate epithelial morphogenesis, including cell scattering, branching tubulogenesis, and remodeling of cell-cell adhesion complexes via ectodomain shedding of nectin-1 alpha. HGF is primarily secreted by mesenchymal cells and acts on epithelial cells to regulate proliferation, motility, and morphogenesis. Through its mitogenic, motogenic, and morphogenic activities, HGF plays critical roles in processes such as tissue regeneration, tumor progression, and angiogenesis.