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.
IP: Use at an assay dependent dilution. Inhib: GTX18177 gives 90% inhibition of insulin binding adipocytes. Shown to activate receptor Kinase in receptor kinase assay. Not tested in other applications. Optimal dilutions/concentrations should be determined by the end user.
Type: Primary
Antigen: INSR
Clonality: Monoclonal
Clone: 1.B.109
Conjugation: Unconjugated
Epitope:
Host: Mouse
Isotype: IgG2a
Reactivity: Human