Background
Insulin-like growth factor I (IGF1) belongs to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mouse IGF-I is synthesized as two precursor isoforms with alternate N- and C-terminal propeptides. These isoforms are differentially expressed by various tissues. Mature mouse IGF-I shares 94% and 99% aa sequence identity with human and rat IGF-I, respectively, and exhibits cross-species activity. It shares 60% aa sequence identity with mature mouse IGF-II. IGF-I induces the proliferation, migration, and differentiation of a wide variety of cell types during development and postnatally. It plays an important role in muscle regeneration and tumor progression. IGF-I binds IGF-I R, IGF-II R, and the insulin receptor. IGF-I association with IGF binding proteins increases its plasma half-life and modulates its interactions with receptors.
Description
IGFS is a mitogenic polypeptide growth factor that stimulates the proliferation and survival of a variety of cells, including muscle, bone, and cartilage tissue. isolated. IGFS is primarily produced by the liver, although different tissues produce IGFS at different times. IGFS belongs to the insulin gene family, which also contains insulin and relaxin. IGFS is similar to insulin in structure and function, but its growth-promoting activity is significantly higher than that of insulin. The expression of IGF-II is affected by placental lactogen, and the expression of IGF-I is regulated by growth hormone. IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), while IGF-II Also signals through the IGF-II/mannose-6-phosphate receptor. Mature IGFS is produced by proteolysis of an inactive precursor protein containing N-terminal and C-terminal precursor regions. Recombinant human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids and 3 intramolecular disulfide bonds, respectively. IGF-ILR3 is a recombinant analog of human IGF-I, consisting of the complete IGF-I sequence , the third glutamic acid is replaced by arginine, and the N-terminal peptide is extended by 13 amino acids. Engineered for higher biological potency, the increased half-life of ex vivo IGF-ILR 3 and its binding aversion to native proteins in vivo make it ideal for research and large-scale culture.
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