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Human HGF Recombinant Protein Lyophilized
Human HGF Recombinant Protein Lyophilized
SKU:IHUHGFRLY5UG
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Key facts
- Species: Human
- Target: HGF
- Purity: ? 95% by SDS-PAGE gel and HPLC analyses.
- Source: HEK293 cells
- Storage 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.
In-depth information
Certificate of Analysis
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Human HGF Recombinant Protein Lyophilized from Innovative Research has been recombinantly produced in HEK293 cells. This is a Lyophilized protein buffered in with a purity of ? 95% by SDS-PAGE gel and HPLC analyses..
More Details:
- Species: Human
- Target: HGF
- Purity: ? 95% by SDS-PAGE gel and HPLC analyses.
- Source: HEK293 cells
- Storage 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.
Additional Information:
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 (?-chain and ?-chain) held together by a single disulfide bond resulting in formation of a biologically active heterodimer. The ?-chain consists of 463 amino acid residues and four kringle domains. The ?-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.
. At Innovative Research we provide reliable, consistent products that deliver reliable, consistent results.
This material is sold for in-vitro use only for manufacturing and research. This material is not suitable for human or animal use. While we make every effort to ensure the safety of our products, we recommend handling any biological materials with standard precautions as if capable of spreading infectious disease. The statements herin are offered for informational purposes only to be used solely for your consideration, investigation, and verification.
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