IGF-I, human recombinant

Human IGF-1 (insulin-like Growth Factor-1, IGF1, MGF, Somatomedin) is a hormone similar in molecular structure to insulin. It is a polypeptide growth factor that stimulates the proliferation of a wide range of cell types including muscle, bone, and cartilage tissue. Insulin-like growth factor 1 has been shown to bind and interact with all the IGF-1 Binding Proteins (IGFBPs), of which there are six (IGFBP1-6). IGFBP-3, the most abundant protein, accounts for 80% of all IGF binding. IGF-1 binds to IGFBP-3 in a 1:1 molar ratio. IGF-1 binds to at least two cell surface receptors: the IGF-1 receptor (IGF1R), and the insulin receptor. The IGF-1 receptor seems to be the "physiologic" receptor - it binds IGF-1 at significantly higher affinity than the IGF-1 that is bound to the insulin receptor. Mature human IGF I shares 94% and 96% aa sequence identity with mouse IGF1 and rat IGF1, respectively, and exhibits cross species activity. It shares 64% aa sequence identity with mature human IGFII. Human IGF-1 is a 7.6 kDa protein containing 70 amino acid residues. The recombinant human IGF-1 was produced using animal origin free technology.