Cell Signaling Technology
XP Monoclonal Antibody

Product Pathways - Metabolism

IGF-I Receptor β (D23H3) XP® Rabbit mAb (Biotinylated) #8521

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

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

Protocols

Specificity / Sensitivity

IGF-I Receptor β (D23H3) XP® Rabbit mAb (Biotinylated) detects endogenous levels of total IGF-I receptor β protein. This antibody does not cross-react with insulin receptor.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human IGF-I receptor β protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from MCF7, 293 (IGF-I receptor β+), and SK-UT-1 (IGF-I receptor β-) cells using IGF-I Receptor β (D23H3) XP® Rabbit mAb (Biotinylated). Streptavidin-HRP #3999 was used for detection.

Description

This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated IGF-I Receptor β (D23H3) XP® Rabbit mAb #9750.

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

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

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