Cell Signaling Technology

Product Pathways - Metabolism

Phospho-IGF-I Receptor β (Tyr980) (C14A11) Rabbit mAb #4568

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

Applications Key:  W=Western Blotting
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 (Tyr980) (C14A11) Rabbit mAb detects endogenous levels of IGF-I β receptor protein when phosphorylated at Tyr980. The antibody may cross-react with activated insulin receptors and FLT3.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr980 of human IGF-I Receptor β.

Western Blotting

Western Blotting

Western blot analysis of extracts from MCF-7 cells, untreated or IGF-I-treated, using Phospho-IGF-I Receptor β (Tyr980) (C14A11) Rabbit mAb (upper) and 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 at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).

Tyr980 of IGF-IR appears to be important for receptor kinase activation. Located in the IGF-IR juxtamembrane region, phosphorylation of this tyrosine residue creates a docking site for the binding of downstream adaptor or docking proteins (9).

  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. Pautsch, A. et al. (2001) Structure 9, 955-965.

Application References

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

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