This Antibody was verified by Cell treatment to ensure that the antibody binds to the antigen stated. View Details
This antibody has been negatively preadsorbed using a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated Insulin Receptor. The final product is generated by affinity chromatography using a Insulin Receptor-derived peptide that is phosphorylated at tyrosine 1334.
This antibody recognizes human insulin receptor phosphorylated at tyrosine 1334 as well as the human IR Isoform B phosphorylated at tyrosine 1332.
Western blot positive control used was insulin-treated CHO-T cells expressing Human Insulin Receptor.
INSR (insulin receptor, IR) is a heterodimeric protein complex that has an intracellular beta subunit and an extracellular alpha subunit, which is disulfide- linked to a transmembrane segment. The insulin ligand binds to the IR and initiates molecular signaling pathways that promote glucose uptake in cells and glycogen synthesis. Insulin binding to IR induces phosphorylation of intracellular tyrosine kinase domains and recruitment of multiple SH2 and SH3 domain-containing intracellular proteins that serve as signaling intermediates for pleiotropic effects of insulin. INSR and IGF-1 receptors share major structural and functional similarity. The earliest cellular response to insulin stimulation is autophosphorylation of tyrosine in INSR. In humans, the INSR gene is located on chromosome 19. Defects in INSR are the cause of various insulin resistance syndromes and IGF-1R defects may also cause some forms of growth retardation.
Protein Aliases: CD 220; CD220; CD220 antigen; CD220 beta; HHF 5; Insulin receptor; insulin receptor preproprotein; Insulin receptor subunit alpha; Insulin receptor subunit beta; IR; IR 1; IR beta; IR-1; IR1
Gene Aliases: 4932439J01Rik; CD220; D630014A15Rik; HHF5; INSR; IR; IR-A; IR-B