Anti-Insulin Receptor alpha (IRa), clone 2Q222

The insulin receptor is a tetrameric transmembranous glycoprotein composed of two alpha subunits (120kD) and two beta subunits (90kD). The alpha subunits are disulfide linked, totally extracellular and are the insulin binding site. The beta subunits are transmembranous and contain an intracellular tyrosine kinase domain. The biological effects of insulin are mediated primarily through the insulin receptor. The interaction of insulin with the alpha-subunit of the insulin receptor activates the protein tyrosine kinase of the beta-subunit which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adaptor proteins, IRS-1, IRS-2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain-containing signaling proteins. Insulin Receptor, alpha (IRa) is a heterotetrameric membrane glycoprotein consisting of disulfide-linked subunits. The alpha subunit (95kD) possesses a single transmembrane domain, whereas the beta-subunit is completely extracellular. The intracellular portion of the alpha subunit is a tyrosine-specific protein kinase with sequence homology to other such kinases. Activation of kinase is essential in signaling pathway whereby insulin regulates intracellular metabolism. Applications: Suitable for use in inhibiting insulin binding. Other applications have not been tested. Recommended Dilution: Use antibody at 10nM, Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.