Product Pathways - Nuclear Receptor Signaling
Phospho-Estrogen Receptor alpha (Ser118) (16J4) Mouse mAb #2511
| Applications | Reactivity | MW (kDa) | Source | Isotype |
|---|---|---|---|---|
| W IHC-P | H | 66 | Mouse | IgG2b |
Applications Key:
W=Western Blotting
IHC-P=Immunohistochemistry (Paraffin)
Reactivity Key:
H=Human
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.
Specificity / Sensitivity
Phospho-Estrogen Receptor alpha (Ser118) (16J4) Mouse mAb detects endogenous levels of estrogen receptor alpha only when phosphorylated at serine 118. It does not cross-react with phosphorylated estrogen receptor beta.
Source / Purification
Monoclonal antibody is produced by immunizing mice with a synthetic phospho-peptide (KLH coupled) corresponding to residues surrounding Ser118 of human ER alpha.
Western Blotting
Western blot analysis of extracts from untransfected MCF-7 cells, and COS-1 cells transfected with wild-type or mutant ER alpha, stimulated with EGF and E2, using Phospho-Estrogen Receptor alpha (Ser118) (16J4) Mouse mAb (upper) or control estrogen receptor alpha antibody #2512 (lower).
IHC-P (paraffin)
Immunohistochemical staining of phosphorylated estrogen receptor alpha in paraffin-embedded human breast carcinoma showing nuclear localization, using Phospho-Estrogen Receptor alpha (Ser118) (16J4) Mouse mAb.
Background
Estrogen receptorα (ER α), a member of the steroid receptor superfamily, contains highly conserved DNA binding (DBD) and ligand binding domains (LBD) (1). Through its estrogen-independent and estrogen-dependent activation domains (AF-1 and AF-2, respectively), ER α regulates transcription by recruiting coactivator proteins and interacting with general transcriptional machinery (2). Phosphorylation provides an important mechanism to regulate ER α activity (3,4). ER α is phosphorylated on multiple sites (5). Serines 104, 106, 118 and 167 are located in the amino-terminal transcription activation function domain AF-1, and phosphorylation of these serines plays an important role in regulating ER α activity. Ser118 may be the substrate of the transcription regulatory kinase cdK7 (5). Ser167 may be phosphorylated by p90RSK and Akt (4,6). Phosphorylation of Ser167 may confer tamoxifen resistance in breast cancer patients (4).
- Mangelsdorf, D.J. et al. (1995) Cell 83, 835-839.
- Glass, C.K. and Rosenfeld, M.G. (2000) Genes Dev. 14, 121-141.
- Chen, D. et al. (1999) Mol. Cell. Biol. 19, 1002-1015.
- Campbell, R.A. et al. (2001) J. Biol. Chem. 276, 9817-9824.
- Chen, D. et al. (2000) Mol. Cell 6, 127-137.
- Joel, P.B. et al. (1998) Mol. Cell. Biol. 18, 1978-1984.
Application References
- Murphy, L. et al. (2004) Phospho-Serine-118 Estrogen Receptor-alpha Detection in Human Breast Tumors in Vivo. Clinical Cancer Research 10, 1354-1359. This article references the use of Phospho-Estrogen Receptor alpha (Ser118) (16J4) Mouse mAb in the following applications: IHC-P (paraffin)
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