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Tyrosine Kinases / Adaptors

EGF Receptor (D38B1) XP™ Rabbit mAb (Biotinylated) #6627

Item # Description List Price Web Price QTY Buy
6627S EGF Receptor (D38B1) XP™ Rabbit mAb (Biotinylated) - 100ul $399.00 $359.10
Applications Reactivity Sensitivity MW (kDa) Source
W H M Mk Endogenous 175 Rabbit

Applications Key:   W = Western Blotting
Reactivity Key: H = Human  M = Mouse  Mk = Monkey  
Species cross-reactivity is determined by Western blot.

Protocols

Specificity / Sensitivity

EGF Receptor (D38B1) XP™ Rabbit mAb (Biotinylated) detects endogenous levels of total EGF receptor protein. The antibody does not cross-react with other proteins of the ErbB family.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a fusion protein containing the cytoplasmic domain of human EGF receptor protein.

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 unconjugated EGF Receptor (D38B1) XP™ Rabbit mAb #4267.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa and A-431 cells using EGF Receptor (D38B1) XP™ Rabbit mAb (Biotinylated) and developed using Streptavidin-HRP #3999.

Background

The epidermal growth factor (EGF) receptor is a 170 kDa transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization and lysosomal degradation (1,2). Phosphorylation of EGF receptor (EGFR) at Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the active state enzyme and providing a binding surface for substrate proteins (3,4). c-Src is involved in phosphorylation of EGFR at Tyr845 (5). The SH2 domain of PLCγ binds at phospho-Tyr992, resulting in activation of PLCγ-mediated downstream signaling (6). Phosphorylation of EGFR at Tyr1045 creates a major docking site for c-Cbl, an adaptor protein that leads to receptor ubiquitination and degradation following EGFR activation (7,8). The GRB2 adaptor protein binds activated EGFR at phospho-Tyr1068 (9). A pair of phosphorylated EGFR residues (Tyr1148 and Tyr1173) provides a docking site for the Shc scaffold protein, with both sites involved in MAP kinase signaling activation (2). Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II; mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation (10).

  1. Hackel, P.O. et al. (1999) Curr Opin Cell Biol11, 184 - 9.
  2. Zwick, E. et al. (1999) Trends Pharmacol Sci20, 408 - 12.
  3. Cooper, J.A. and Howell, B. et al. (1993) Cell73, 1051 - 4.
  4. Hubbard, S.R. et al. (1994) Nature372, 746 - 54.
  5. Biscardi, J.S. et al. (1999) J Biol Chem274, 8335 - 43.
  6. Emlet, D.R. et al. (1997) J Biol Chem272, 4079 - 86.
  7. Levkowitz, G. et al. (1999) Mol Cell4, 1029 - 40.
  8. Ettenberg, S.A. et al. (1999) Oncogene18, 1855 - 66.
  9. Rojas, M. et al. (1996) J Biol Chem271, 27456 - 61.
  10. Feinmesser, R.L. et al. (1999) J Biol Chem274, 16168 - 73.

Application References

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Companion Products


This product is for in vitro research use only and is not intended for use in humans or animals. This product is not intended for use as therapeutic or in diagnostic procedures.