Recombinant Human HGF (carrier-free)

Hepatocyte growth factor (HGF )was initially purified from plasma of a patient with fulminant hepatic failure. HGF is a dimeric molecule composed of the α-subunit and β-subunit, linked by a disulfide bond. The two chains are derived from a precursor encoded by the same open reading frame. The C-terminus of the α-subunit is followed directly by the N-terminus of the β-subunit. The pro-HGF possesses 728 amino acids and the subunits are formed by proteolytic cleavage. Proteolytic activation of the precursor form in the extracellular milieu is performed by HGF activator (HGFA). HGFA is a factor XII-like serine proteinase that is not inhibited by serum proteinase inhibitors. Two inhibitors have been described for HGFA, HGFA inhibitor type 1 and type 2 (HAI-1 and -2). Both inhibitors have two well-defined Kunitz inhibitor domains and a presumed transmembrane domain. HGF protects the epithelium, neurons and cardiomyocytes during organ diseases; this protective effect is mediated through anti-apoptotic signals via inhibition of caspase-3 activity or induction of anti-apoptotic molecules, such as Bcl-xL. In addition, HGF prohibits Fas-mediated apoptosis signals via sequestration of Fas and Met receptor on cell surfaces. Also, HGF elicits the regression of fibrosis in numerous organs, such as scleroderma, cardiomyopathy, vocal scarring, and peritoneal fibrosis.