HGF, Human, HEK293 Cells,Tag Free

FHepatocyte Growth Factor (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 (1-5). 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 (6, 7). HGF-dependent c-MET activation is implicated in the development of many human cancers (8). HGF regulates epithelial morphogenesis by inducing cell scattering and branching tubulogenesis (9, 10). HGF induces the up-regulation of integrin alpha 2 beta 1 in epithelial cells by a selective

increase in alpha 2 gene transcription (11). This integrin serves as a collagen I receptor, and its blockade disrupts epithelial cell branching tubulogenesis (11, 12). HGF can also alter epithelium morphology by the induction of nectin-1 alpha  ectodomain shedding, an adhesion protein component of adherens junctions (13). In the thyroid, HGF induces the proliferation, motility, and loss of differentiation markers of thyrocytes and inhibits TSH-stimulated iodine

uptake (14). HGF promotes the motility of cardiac stem cells in damaged myocardium (15).

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