HGFAC belongs to peptidase family S1. It is first synthesized as an inactive single-chain precursor before being activated to a heterodimeric form by endoproteolytic processing. It acts as serine protease that converts hepatocyte growth factor to the active form. Miyazawa et al. (1993) determined the partial amino acid sequence of the homologous human serine protease and used it to design degenerate primers to screen a human liver cDNA library. They identified a 655-amino acid inactive precursor protein, designated hepatocyte growth factor activator (HGFAC), with a calculated molecular mass of 70,681 Da. They determined that the active protein purified from serum is derived from the C terminus of the precursor by proteolytic cleavage of the bonds between arg372-val373 and arg407-ile408.
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