Cell Signaling Technology

Product Pathways - Nuclear Receptor Signaling

Phospho-Estrogen Receptor α (Ser104/106) Antibody #2517

Applications Reactivity Sensitivity MW (kDa) Source
W H (M) Endogenous 66 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse
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 alpha (Ser104/106) Antibody detects endogenous levels of ER alpha only when phosphorylated at Ser104/106. It does not cross-react with the phosphorylated ER isoform beta.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding serine 104/106 of human ER alpha. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from COS-1 cells expressing wild-type or mutant ER alpha, stimulated with beta-estradiol (100 nM) and EGF (100 ng/ml) for 30 minutes, using Phospho-Estrogen Receptor alpha (Ser104/106) Antibody (upper) or control ER alpha Antibody #2512 (lower). (Cell lysates provided by Dr. Simak Ali, Hammersmith Hospital, London.)

Western Blotting

Western Blotting

Western blot analysis of extracts from serum-starved MCF7 cells, untreated, treated with β-estradiol, or treated with β-estradiol and heregulin, using Phospho-Estrogen Receptor α (Ser104/106) Antibody. A non-specific band is detected at 90 kDa.

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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