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 that is 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 tyrosine 1158 (tyrosine 1131 for IGF1R).
CHO-T transfected with a vector containing insulin receptor and stimulated with insulin was used as positive control.
The immunogenic sequence is conserved in mouse and rat for both the IR and IGF1R; this antibody is expected to react in human, mouse, and rat, and has been used in western blotting and immunostaining.
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 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; JTK13; soluble IGF1R variant 1; soluble IGF1R variant 2
Gene Aliases: CD220; CD221; HHF5; IGF1R; IGFIR; IGFR; INSR; JTK13