This Antibody was verified by Cell Treatment to ensure that the antibody binds to the antigen stated. View Details
The antibody has been negatively preadsorbed using a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody reactive with non-phosphorylated insulin/insulin-like growth factor-1 receptor (IR/IGF1R). The final product is generated by affinity chromatography using an IR/IGF1R-derived peptide that is phosphorylated at tyrosines 1162 and 1163 (tyrosines 1135 and 1136 for IGF1R. The antiserum was produced against a chemically synthesized phosphopeptide derived from the region of IR/IGF1R that contains tyrosines 1162 and 1163 of the human insulin receptor (IR) as numbered according to Ebina, et al. (1150 and 1151 according to Ullrich et al.). The corresponding residues in the IGF1R are 1135 and 1136. The sequence is conserved in mouse and rat for both the IR and IGF1R. Although exhibiting a preference for IR/IGF1R, this antibody has been shown by both peptide competition and protein blotting to react with other dual-phosphotyrosine motifs from proteins such as c-Met and Shc.
This antibody has been used in western blotting and previous lots of this antibody have been used in immunostaining. Positive controls used with this antibody in western analysis were Chinese hamster ovary cells transfected with a vector containing human insulin receptor (CHO-T) and stimulated with insulin, or 3T3-L1 cells stimulated with insulin.
Biological actions of insulin and IGF-1 are mediated by their respective cell surface receptors, both of which are receptor tyrosine kinases that regulate multiple signaling pathways through activation of a series of phosphorylation cascades. The IR and IGF-1R are heterotetrameric proteins consisting of two ligand-binding alpha subunits, which are completely extracellular, and two beta subunits that span the membrane with an intracellular portion that each contain a tyrosine kinase domain. These disulfide-linked subunits are in a beta-alpha-alpha-beta configuration in the mature receptor. Insulin/IGF-1 binding to the extracellular domain leads to autophosphorylation of the receptor and activation of the intrinsic tyrosine kinase activity, which allows appropriate substrates to be phosphorylated. These two receptors differ in sequence in regions that confer specificity for the designated ligand as well as in certain intracellular signaling domains. These differences allow insulin and IGF-1 to regulate different physiological functions through receptors that share a very similar structure. Phosphorylation sites that are unique to each receptor presumably play a key role in these signaling differences. The catalytic loops within the tyrosine kinase domains of the IR/IGF-1R contain a three tyrosine motif corresponding to tyrosines 1158, 1162, and 1163 (for the IR) and tyrosines 1131, 1135, and 1136 (for the IGF-1R). It is generally believed that autophosphorylation within the activation loop proceeds in a processive manner initiating at the second tyrosine (1162 or 1135), followed by phosphorylation at the first tyrosine (1158 or 1131), then the last (1163 or 1136), upon which the IR or IGF-1R becomes fully active.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: CD220; CD221; HHF5; IGF-I Receptor; IGF1 Receptor; IGF1R; IGFIR; IGFR; INSR; Insulin receptor; Insulin-like growth factor 1 receptor; Insulin-like growth factor I receptor; IR; JTK13; soluble IGF1R variant 1; soluble IGF1R variant 2
Gene Aliases: CD220; CD221; HHF5; IGF1R; IGFIR; IGFR; INSR; JTK13