Human insulin-like growth factor-I (IGF-I) is a single chain 70 amino acid polypeptide that shares structural homology with insulin and human IGF-II. IGF-I plays a critical role in growth, differentiation and development via autocrine, paracrine and endocrine mechanisms. It is a mitogen and also has effects on cell migration and differentiation. IGF-I binds to the type I IGF receptor and most of its actions are probably mediated through inducing signal transduction via this receptor. IGF-I also binds to each of the six IGF binding proteins (IGFBPs). This binding also regulates the biological function of IGF-I. IGF-I is highly conserved across species which suggests an important role for the peptide. Human IGF-I is present in high concentrations in normal adult human serum in a complex with IGFBP-3 and the acid-labile subunit (ALS) and mediates many of the actions of Growth Hormone. IGF-I is a regulator of metabolism and is also implicated in the pathophysiology of cancer, diabetes and obesity.

Media grade human IGF-I is a high quality reagent at an economical cost to enable studies where higher quantities of peptide are required.