Cell Signaling Technology

Product Pathways - Nuclear Receptor Signaling

Phospho-Estrogen Receptor α (Ser167) (D1A3) Rabbit mAb #5587

Applications Reactivity Sensitivity MW (kDa) Isotype
W H (Mk) Endogenous 66 Rabbit IgG

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  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

Phospho-Estrogen Receptor α (Ser167) (D1A3) Rabbit mAb detects endogeneous levels of ERα protein only when phosphorylated at Ser167. The antibody cross reacts with a nonspecific band at around 77 kDa.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser167 of human estrogen receptor α protein.

Western Blotting

Western Blotting

Western analysis of extracts from MCF7 cells, untreated or treated with Estrodiol/EGF (100nM each, together for 30 min) and further treated with calf intestinal phosphatase (CIP), using Phospho-Estrogen Receptor α (Ser167) (D1A3) Rabbit mAb (upper) or Estrogen Receptor α (D62A3) Mouse mAb (lower).

Background

Estrogen receptor α (ERα), a member of the steroid receptor superfamily, contains highly conserved DNA binding and ligand binding domains (1). Through its estrogen-independent and estrogen-dependent activation domains (AF-1 and AF-2, respectively), ERα regulates transcription by recruiting coactivator proteins and interacting with general transcriptional machinery (2).Phosphorylation at multiple sites provides an important mechanism to regulate ERα activity (3-5). Ser104, 106, 118, and 167 are located in the amino-terminal transcription activation function domain AF-1, and phosphorylation of these serine residues plays an important role in regulating ERα activity. Ser118 may be the substrate of the transcription regulatory kinase CDK7 (5). Ser167 may be phosphorylated by p90RSK and Akt (4,6). According to the research literature, phosphorylation at Ser167 may confer tamoxifen resistance in breast cancer patients (4).

  1. Mangelsdorf, D.J. et al. (1995) Cell 83, 835-839.
  2. Glass, C.K. and Rosenfeld, M.G. (2000) Genes Dev. 14, 121-141.
  3. Chen, D. et al. (1999) Mol. Cell. Biol. 19, 1002-1015.
  4. Campbell, R.A. et al. (2001) J. Biol. Chem. 276, 9817-9824.
  5. Chen, D. et al. (2000) Mol. Cell 6, 127-137.
  6. Joel, P.B. et al. (1998) Mol. Cell. Biol. 18, 1978-1984.

Application References

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Companion Products

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

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