HGF Recombinant Protein

HGF is a potent, mesenchymally-derived mitogen for mature parenchymal hepatocytes, and acts as a growth factor for a broad spectrum of tissues and cell types. HGF signals through a transmembrane tyrosine kinase receptor known as MET. Activities of HGF include the induction of cell proliferation, motility, morphogenesis, inhibition of cell growth, and enhancement of neuron survival. HGF is a crucial mitogen for liver regeneration processes, especially after partial hepatectomy and other liver injuries. Human and murine HGF are cross-reactive. Human HGF is expressed as a linear, polypeptide-precursor glycoprotein containing 697 amino acid residues. Proteolytic processing of this precursor generates the biologically active heterodimeric form of HGF, which consists of two polypeptide chains (α-chain and β-chain) held together by a single disulfide bond resulting in formation of a biologically active heterodimer. The α-chain consists of 463 amino acid residues and four kringle domains. The β-chain consists of 234 amino acid residues. Recombinant Human HGF, sourced from HEK293 cells, is a 79.4 kDa polypeptide consisting of 695 amino acid residues. As a result of glycosylation, Recombinant Human HGF migrates with an apparent molecular mass of approximately 68-85 kDa by SDS-PAGE gel, under non-reducing conditions.

The recombinant protein is stable for at least 2 years from date of receipt at -20˚ C. Reconstituted protein is stable for at least 3 months when stored in working aliquots with a carrier protein at -20˚ C. As with any protein, exposing the recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.