IGFBP3 (H-98) Antibody: sc-9028

IGFBP3 Background Information
The insulin-like growth factor-binding proteins, or IGFBPs, are a family of homologous proteins that have co-evolved with the IGFs. They serve not only as shuttle molecules for the soluble IGFs, but also confer a level of regulation to the IGF signaling system. Physical association of the IGFBPs with IGF influences the bio-availability of the growth factors, as well as their concentration and distribution in the extracellular environment. In addition, the IGFBPs appear to have biological activity independent of the IGFs. Seven IGFBPs have thus far been described, each differing in their tissue distribution, half-lives and modulation of IGF interactions with their receptors. For instance, IGFBP1 is negatively regulated by insulin production. The IGFBP1 gene is expressed at a high level during fetal liver development and in response to nutritional changes and diabetes. It has been suggested that IGFBP2 functions as chaperone, escorting IGFs to their target tissues. It is expressed in several human tissues including fetal eye and fetal brain. IGFBP3 is the most abundant IGFBP and is complexed with roughly 80% of the serum IGFs. Both IGFBP3 and IGFBP4 are released by dermal fibroblasts in response to incision injury. IGFBP5 is secreted by myoblasts and may play a key role in muscle differentiation. IGFBP6 differs from other IGFBPs in having the highest affinity for IGF-II. Glycosylated human IGFBP6 is expressed in Chinese hamster ovary (CHO) cells, whereas nonglycosylated recombinant human IGFBP6 is expressed in E.coli. IGFBP7 is a secreted protein and binds both IGF-I and IGF-II with a relatively low affinity. It stimulates prostacyclin production and may also function as a growth-suppressing factor.