IGF-1 (human), animal-free recombinant

The IGFs are polypeptide growth factors with mitogenic properties, stimulating cell proliferation and survival in various tissues like muscle, bone, and cartilage when studied in vitro. Although primarily produced in the liver, different tissues produce IGFs at specific times. Belonging to the Insulin gene family, which also includes insulin and relaxin, IGFs share structural and functional similarities with insulin but possess significantly stronger growth-promoting abilities. The expression of IGF-II 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), yet IGF-II can also utilize the IGF-II/Mannose-6-phosphate receptor for signaling. Mature IGFs are formed through proteolytic processing of inactive precursor proteins that contain N-terminal and C-terminal propeptide regions. Recombinant Human IGF-I and IGF-II are globular proteins composed of 70 and 67 amino acids, respectively, with three intra-molecular disulfide bonds. The estimated molecular weight of Recombinant Human IGF-I is 7.6 kDa. Product Specifications Species Human Published Species Human, Mouse, Rat, Salamander Expression System E.coli Amino Acid Sequence GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA Molecular Weight 7.6 kDa Class Recombinant Type Protein Purity > 98% by SDS-PAGE gel and HPLC analyses. Endotoxin Concentration <0.1 EU/µg Activity The ED50 was determined by a cell proliferation assay using FDC-P1 cells is = 2.0 ng/ml, corresponding to a specific activity of > 5 x 105 units/mg. Conjugate Unconjugated Form Lyophilized Contains No Preservative Storage -20°C CAUTION For Research Use Only. Not for use in diagnostic procedures.Protein function: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]- 2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake. May play a role in synapse maturation (PubMed:21076856, PubMed:24132240). Ca(2+)-dependent exocytosis of IGF1 is required for sensory perception of smell in the olfactory bulb. Acts as a ligand for IGF1R. Binds to the alpha subunit of IGF1R, leading to the activation of the intrinsic tyrosine kinase activity which autophosphorylates tyrosine residues in the beta subunit thus initiatiating a cascade of down-stream signaling events leading to activation of the PI3K-AKT/PKB and the Ras-MAPK pathways. Binds to integrins ITGAV:ITGB3 and ITGA6:ITGB4. Its binding to integrins and subsequent ternary complex formation with integrins and IGFR1 are essential for IGF1 signaling. Induces the phosphorylation and activation of IGFR1, MAPK3/ERK1, MAPK1/ERK2 and AKT1 (PubMed:19578119, PubMed:22351760, PubMed:23696648, PubMed:23243309). [The UniProt Consortium]