Cell Signaling Technology

Product Pathways - Glucose Metabolism

Phospho-IGF-I Receptor β (Tyr1316) Antibody #6113

Applications Reactivity Sensitivity MW (kDa) Source
W IP H M R Endogenous 95 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human  M=Mouse  R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Phospho-IGF-I Receptor β (Tyr1316) Antibody detects endogenous levels of IGF-I receptor only when phosphorylated at Tyr1316. This antibody may also cross-react with other overexpressed, related tyrosine-phosphorylated tyrosine kinases.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr1316 of human IGF-I receptor. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from 293 cells, untreated or treated with IGF-1 (100 nM for 2 minutes), using Phospho-IGF-1 Receptor β (Tyr1316) Antibody (upper) or IGF-I Receptor β (111A9) Rabbit mAb #3018 (lower).

Background

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 of Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).

Phosphorylation of IGF-I receptor on Tyr1346 (equivalent to Tyr1316 in mature protein) was identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's LC-MS/MS platform for phosphorylation site discovery (9). Phosphorylation of IGF-I receptor on Tyr1346 was also reported by several other labs in select carcinoma cell lines (10,11).

  1. Adams, T.E. et al. (2000) Cell. Mol. Life Sci. 57, 1050-1093.
  2. Baserga, R. et al. (2000) Oncogene 19, 5574-5581.
  3. Scheidegger, K.J. et al. (2000) J. Biol. Chem. 275, 38921-38928.
  4. Hernandez-Sanchez, C. et al. (1995) J. Biol. Chem. 270, 29176-29181.
  5. Lopaczynski, W. et al. (2000) Biochem. Biophys. Res. Commun. 279, 955-960.
  6. Baserga, R. et al. (1999) Exp. Cell Res. 253, 1-6.
  7. White, M.F. et al. (1985) J. Biol. Chem. 260, 9470-9478.
  8. White, M.F. et al. (1988) J. Biol. Chem. 263, 2969-2980.
  9. Rush, J. et al. (2005) Nat Biotechnol 23, 94-101.
  10. Peterson, J.E. et al. (1996) J Biol Chem 271, 31562-71.
  11. Knowlden, J.M. et al. (2005) Endocrinology 146, 4609-18.

Application References

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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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