IGF-I Receptor α (D3A2W) Rabbit mAb #17174

The type 1 insulin-like growth factor receptor (IGF1R) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell types in fetal and postnatal tissues, and which is highly similar in sequence and structure to the insulin receptor (1-4). IGF1R is synthesized as a preproprotein which is proteolytically cleaved into alpha and beta subunits. Receptor assembly involves heterodimerization of two alpha and two beta subunits to generate the heterotetrameric transmembrane receptor. The alpha subunits form the extracellular ligand binding domain; ligand binding by IGF-I or IGF-II initiates autophosphorylation of conserved intracellular residues in the beta subunit kinase domain, leading to kinase activation and subsequent activation of downstream signal transduction pathways (e.g., Akt and MAPK) (4-8). Enhanced mitogenic signaling through the IGF1R is frequently observed in cancer, making the IGF1R an important research target in translational oncology (9).