Cell Signaling Technology

Product Pathways - Tyrosine Kinase/ Adaptors

SignalSlide™ Phospho-EGF Receptor (Tyr1173) IHC Controls #8102

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Description

Each control slide contains formalin fixed, paraffin-embedded MDA-MB-468 cells, both untreated and treated with EGF, that serve as a control for Phospho-EGFR(Tyr1173) immunostaining. Western blot analysis was performed on extracts derived from the same cells to verify the efficacy of the EGF treatment.

Western Blotting

Western Blotting

Western blot analysis of extracts from MDA-MB-468 cells, untreated or treated with EGF, using Phospho-EGF Receptor (Tyr 1173) (53A5) Rabbit mAb #4407 (upper) or EGF Receptor Antibody #2232 (lower). This assay serves as a control for the efficacy of the EGF treatment.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded MDA-MB-468 cells, untreated (left) or treated with EGF (right), using Phospho-EGF Receptor (Tyr1173) (53A5) Rabbit mAb #4407.

Applications

These slides are intended for use in immunohistochemical assays. Please see the Companion Products for a list of products that can be used with these slides.

Companion Products

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 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 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; mutations to either of these serines results in upregulated EGFR tyrosine autokinase activity (10).

  1. Hackel, P.O. et al. (1999) Curr. Opin. Cell Biol. 11, 184-189.
  2. Zwick, E. et al. (1999) Trends Pharmacol. Sci. 20, 408-412.
  3. Cooper, J.A. and Howell, B. (1993) Cell 73, 1051-1054.
  4. Hubbard, S.R. et al. (1994) Nature 372, 746-754.
  5. Biscardi, J.S. et al. (1999) J. Biol. Chem. 274, 8335-8343.
  6. Emlet, D.R. et al. (1997) J. Biol. Chem. 272, 4079-4086.
  7. Levkowitz, G. et al. (1999) Mol. Cell 4, 1029-1040.
  8. Ettenberg, S.A. et al. (1999) Oncogene 18, 1855-1866.
  9. Rojas, M. et al. (1996) J. Biol. Chem. 271, 27456-27461.
  10. Feinmesser, R.L. et al. (1999) J. Biol. Chem. 274, 16168-16173.

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