Human, Mouse IGF-I-LR3 Recombinant Protein (Animal Free) Lyophilized from Innovative Research has been recombinantly produced in E. coli. This is a Lyophilized protein buffered in with a purity of ? 98% by SDS-PAGE gel and HPLC analyses..
More Details:
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Species: Human, Mouse
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Target: IGF1
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Purity: ? 98% by SDS-PAGE gel and HPLC analyses.
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Source: E. coli
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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:
The IGFs are mitogenic, polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone, and cartilage tissue in vitro. IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar to insulin by structure and function, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids, respectively, and 3 intra-molecular disulfide bonds. IGF-I LR3 is a recombinant analog of human IGF-I comprised of the complete IGF-I sequence, with an Arginine substitution for the third position Glutamic acid, and a 13 amino acid length N terminal peptide extension. Specifically engineered for higher biological potency in vitro, IGF-I LR3 has an increased half-life and a binding aversion to native proteins within the body that make it ideal for both research and large-scale culturing. Recombinant Human IGF-I LR3 is a 9.1 kDa, single, non-glycosylated polypeptide chain containing 83 amino acid residues.
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