Cell Signaling Technology

Product Pathways - Metabolism

Phospho-IGF-I Receptor β (Tyr1135/1136)/Insulin Receptor β (Tyr1150/1151) (19H7) Rabbit mAb #3024

Applications Reactivity Sensitivity MW (kDa) Isotype
W H M R (B) Endogenous 95 Rabbit IgG

Applications Key:  W=Western Blotting
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.

Protocols

Specificity / Sensitivity

Phospho-IGF-I Receptor β (Tyr1135/1136)/Insulin Receptor β (Tyr1150/1151) (19H7) Rabbit mAb detects endogenous levels of IGF-I receptor and insulin receptor only when phosphorylated at tyrosine 1135/1136 or tyrosine 1150/1151, respectively. It does not cross-react with other related tyrosine-phosphorylated tyrosine kinases.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr1135/1136 of human IGF-I receptor β.

Western Blotting

Western Blotting

Western blot analysis of untreated and IGF-treated Hela cell extracts as well as untreated and insulin-treated H-4-II-E cell extracts using Phospho-IGF-I-Receptor beta (Tyr1135/1136)/Insulin Receptor beta (Tyr1150/1151)(19H7) Rabbit mAb

Western Blotting

Western Blotting

Phospho-IGF-I Receptorβ (Tyr1135/1136)/Insulin Receptor β (Tyr1150/1151) (19H7) Rabbit mAb specifically binds to tyrosine phosphorylated IGF-1 and insulin receptors, but not other phosphorylated tyrosine kinases. Western blot analysis of of extracts from cells expressing different activated tyrosine kinase proteins, using Phospho-IGF-I Receptor β (Tyr1135/1136)/Insulin Receptor β(Tyr1150/1151) (19H7) Rabbit mAb (upper) or Phospho-Tyrosine Mouse mAb (P-Tyr-100) #9411 (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 at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).

  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.

Application References

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Companion Products

Rabbit Monoclonals Produced Using Epitomics® Technology, U.S. Patent No. 5,675,063.

For Research Use Only. Not For Use In Diagnostic Procedures.

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