Insulin-like Growth Factor II (IGF-II) is a single chain 7 kDa polypeptide, and shares a high degree of homology with insulin. During circulation in vivo, IGF-II is complexed to high affinity binding proteins, IGF Binding Proteins (IGFBP), which act as circulating reservoirs, transport IGF-II, and prolong the half life of IGF-II. The receptors of IGF-II (IGFRs) are transmembrane tyrosine receptors, and are heterotetrameric consisting of two a-subunits and two ß-subunits. IGFRs execute their role via intracellullar signaling molecules, such as IRS, shc, and PI3K. The functions of IGF-II include promoting cell survival, growth, proliferation, differentiation and motility. In particular, IGF-II promotes proliferation, inhibits death, and stimulates transformation in breast cancer cells.
Recombinant human Insulin-like Growth Factor II (rhIGF-II) produced in E. coli is a single non-glycosylated polypeptide chain containing 68 amino acids. A fully biologically active molecule, rhIGF-II has a molecular mass of 7.6 kDa analyzed by reducing SDS-PAGE and is obtained by proprietary chromatographic techniques at GenScript.