Phospho-Insulin Receptor β (Tyr1361) (84B2) Rabbit mAbProduct information
Phospho-Insulin Receptor β (Tyr1361) (84B2) Rabbit mAb
|100 µl (10 western blots)||-||Unavailable in your region|
Product Pathways - Metabolism
Phospho-Insulin Receptor β (Tyr1361) (84B2) Rabbit mAb #3023
|3023S||100 µl (10 western blots)||---||In Stock||---|
|3023||carrier free and custom formulation / quantity||email request|
|W||1:1000||Human||Transfected Only||95||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Specificity / Sensitivity
Phospho-Insulin Receptor β (Tyr1361) (84B2) Rabbit mAb detects transfected levels of insulin receptor β only when phosphorylated at Tyr1361. It slightly cross-reacts with activated IGF-I receptor, but does not cross-react with other activated tyrosine kinases.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr1361 of human insulin receptor β.
Cross-reactivity testing of Phospho-Insulin Receptor (Tyr1361) (84B2) Rabbit mAb with activated IGF-I receptors. Various amounts of activated recombinant IGF-I receptor cytoplasmic domain proteins were applied for Western blot analysis, using Phospho-Insulin Receptor (Tyr1361) (84B2) Rabbit mAb (upper) and Phospho-IGF-I Receptor (Tyr1315/1316) (19H7) Rabbit mAb #3024 (lower) respectively. The result showed that Phospho-Insulin Receptor (Tyr1361) (84B2) Rabbit mAb barely cross-reacts with activated IGF-I receptors.
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, 1050-93.
- Baserga, R. (2000) Oncogene 19, 5574-81.
- Scheidegger, K.J. et al. (2000) J Biol Chem 275, 38921-8.
- Hernández-Sánchez, C. et al. (1995) J Biol Chem 270, 29176-81.
- Lopaczynski, W. et al. (2000) Biochem Biophys Res Commun 279, 955-60.
- Baserga, R. (1999) Exp Cell Res 253, 1-6.
- White, M.F. et al. (1985) J Biol Chem 260, 9470-8.
- White, M.F. et al. (1988) J Biol Chem 263, 2969-80.
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This product is intended for research purposes only. The product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.
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U.S. Patent No. 7,429,487, foreign equivalents, and child patents deriving therefrom.