IGF2 antibody

Insulin-like Growth Factor II (IGFII) was first isolated from human serum by Froesch, et al., as a factor displaying insulin like activities that were not suppressed by antibodies to insulin. It had been discovered that growth hormone dependent factors in serum stimulate the incorporation of 35S into cartilage and that calf serum factors induced cellular division in chick fibroblasts. In 1972, the term ""somatomedin"" was introduced in an unsuccessful attempt to unify the nomenclature of these hormone-dependent factors. In 1987, a consensus among an international group of scientists endorsed the use of the terms insulin like growth factors (IGFI and IGFII), originally proposed by Rinderknecht and Humbel. Hence, IGFI and IGFII have had several synomyms: nonsuppressible insulin like activity (NSIL-A), sulfation factor activity (SFA), and multiplication stimulating activity (MSA). Because IGFII was not regulated by growth hormone, only IGFI was known as a somatomedin. Human IGFII contains 67 amino acids and shares similar structural features with IGFI, including a 62% sequence homology. In human plasma, IGFI and IGFII are associated with IGF-binding proteins that transport the polypeptides and partially regulate their actions in vivo. In addition to the insulin receptor, IGFII binds to two forms of IGF receptors, both of which are widely distributed in different tissues and cultured cells. IGFII is mitogenic for a variety of cultured cells, including mouse 3T3 cells,12 normal rat kidney cells, human or chicken fibroblasts and MCF-7 human breast carcinoma cells.