Mouse HGF Recombinant Protein Lyophilized from Innovative Research has been recombinantly produced in (BTI-Tn-5B1-4) High-5 Insect cells. This is a Lyophilized protein buffered in with a purity of Greater than 95% by SDS-PAGE gel and HPLC analyses..
More Details:
- Species: Mouse
- Target: Hgf
- Purity: Greater than 95% by SDS-PAGE gel and HPLC analyses.
- Source: (BTI-Tn-5B1-4) High-5 Insect cells
- Storage Conditions: The lyophilized HGF recombinant protein is stable for at least 2 years from date of receipt at -20°C. Reconstituted HGF stable for at least 3 months when stored in working aliquots with a carrier protein at -20°C. As with any protein, exposing HGF 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.
Additional Information:
HGF is a mesenchymally derived potent mitogen for mature parenchymal hepatocyte cells 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 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. Murine HGF is expressed as a linear 728 amino acid polypeptide precursor glycoprotein. Proteolytic processing of this precursor generates the biologically active form of HGF, which consists of two polypeptide chains (and#945;-chain and and#946;-chain) held by a single disulfide bond resulting in formation of a biologically active heterodimer. The and#945;-chain consists of 463 amino acid residues and four kringle domains. The and#946;-chain consists of 233 amino acid residues.*Manufactured using (BTI-Tn-5B1-4) cells under license from the Boyce Thompson Institute for Plant Research, Inc.
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