Product Pathways - Nuclear Receptor Signaling
Phospho-Estrogen Receptor α (Ser118) (16J4) Mouse mAb #2511
PhosphoSitePlus® protein, site, and accession data: ER-alpha
| Applications | Reactivity | Sensitivity | MW (kDa) | Isotype |
|---|---|---|---|---|
| W IHC-P | H | Endogenous | 66 | Mouse IgG2b |
Applications Key:
W=Western Blotting
IHC-P=Immunohistochemistry (Paraffin)
Reactivity Key:
H=Human
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Protocols
- 2511:
- IHC / Paraffin, Western Blotting
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 animals with a synthetic phosphopeptide 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 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).
- 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
- Plaza-Menacho, I. et al. (2010) Oncogene 29, 4648-57. Applications: Western Blotting
- Murphy, L. et al. (2004) Phospho-Serine-118 Estrogen Receptor-alpha Detection in Human Breast Tumors in Vivo. Clinical Cancer Research 10, 1354-1359. Applications: IHC-P (paraffin)
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Companion Products
- 2517 Phospho-Estrogen Receptor α (Ser104/106) Antibody
- 7072 Phototope®-HRP Western Blot Detection System, Anti-mouse IgG, HRP-linked Antibody
- 7076 Anti-mouse IgG, HRP-linked Antibody
- 7720 Prestained Protein Marker, Broad Range (Premixed Format)
- 7727 Biotinylated Protein Ladder Detection Pack
- 7003 20X LumiGLO® Reagent and 20X Peroxide
- 9924 Phospho-Estrogen Receptor α Antibody Sampler Kit
For Research Use Only. Not For Use In Diagnostic Procedures.
