Product Pathways - Metabolism
Phospho-IGF-I Receptor β (Tyr1131)/Insulin Receptor β (Tyr1146) Antibody #3021
|W IP||H M R (B)||Endogenous||95||Rabbit|
Reactivity Key: H=Human M=Mouse R=Rat B=Bovine
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
Phospho-IGF-I Receptor β (Tyr1131)/Insulin Receptor β (Tyr1146) Antibody detects endogenous levels of Tyr1131-phosphorylated IGF-I receptor and Tyr1146-phosphorylated insulin receptor. The antibody cross-reacts with activated PDGF, FGF and EGF receptors, ErbB2 and c-Met.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues of human IGF-I Receptor β. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from 293 cells, untreated or IGF-I-treated (100 nM for 2 minutes), using Phospho-IGF-I Receptor β (Tyr1131)/Insulin Receptor β (Tyr1146) Antibody (upper) or control IGF-I Receptor antibody (lower).
Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).
- Adams, T.E. et al. (2000) Cell. Mol. Life Sci. 57, 1050-1093.
- Baserga, R. et al. (2000) Oncogene 19, 5574-5581.
- Scheidegger, K.J. et al. (2000) J. Biol. Chem. 275, 38921-38928.
- Hernandez-Sanchez, C. et al. (1995) J. Biol. Chem. 270, 29176-29181.
- Lopaczynski, W. et al. (2000) Biochem. Biophys. Res. Commun. 279, 955-960.
- Baserga, R. et al. (1999) Exp. Cell Res. 253, 1-6.
- White, M.F. et al. (1985) J. Biol. Chem. 260, 9470-9478.
- White, M.F. et al. (1988) J. Biol. Chem. 263, 2969-2980.
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For Research Use Only. Not For Use In Diagnostic Procedures.