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. \r
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.
Insulin and Insulin-like Growth Factor receptors are transmembrane tyrosine kinase receptors that play critical roles in development, cell growth and metabolism. Insulin/Insulin-like growth factor-1 binding to the extracellular domain of IR and IGFR leads to autophosphorylation of the receptor and activation of the intrinsic tyrosine kinase activity, which allows appropriate substrates to be phosphorylated. 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 contain a three tyrosine motif corresponding to Tyr1158, 1162 and 1163 (for the IR) and Tyr1131, 1135 and 1136 (for the IGF1R). Autophosphorylation of the tyrosine sites within the activation loop proceeds in a processive manner initiating at the second tyrosine (1162 or 1135), followed by phosphorylation at tyrosines 1158 (IGF-1R tyrosine 1131), 1163 (IGF-1R tyrosine 1136), resulting in the full activation of IR and IGF1R.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: CD220; CD221; IGF-I receptor; IGF-I Receptor beta; IGF1 Receptor; IGF1 Receptor beta; IGF1R beta; Insulin receptor; Insulin receptor subunit alpha; Insulin receptor subunit beta; Insulin-like growth factor 1 receptor; Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain; Insulin-like growth factor I receptor; IR; soluble IGF1R variant 1; soluble IGF1R variant 2
Gene Aliases: CD220; CD221; HHF5; IGF1R; IGFIR; IGFR; INSR; JTK13