Estrogen Receptor β Antibody #5513
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- WB
Inquiry Info. # 5513
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Supporting Data
REACTIVITY | H M R Mk |
SENSITIVITY | Endogenous |
MW (kDa) | 52, 55, 63 |
SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
Application | Dilution |
---|---|
Western Blotting | 1:1000 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
Estrogen Receptor β Antibody detects endogenous levels of total Estrogen Receptor β protein. This antibody is predicted to cross-react with all Estrogen Receptor β isoforms. This antibody does not cross-react with Estrogen Receptor α.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human Estrogen Receptor β1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Estrogen Receptor β (ER β) is a member of the nuclear receptor superfamily of transcription factors and was discovered to be encoded by a gene (ESR2) distinct from that encoding Estrogen Receptor α (ER α) (1,2). While studies have revealed that alternative splicing generates mutiple isoforms of ER β that differ at their respective C-termini and in tissue distribution, ER β1 is believed to be the longest and only fully functional isoform (3,4). Indeed, it has been reported that shorter isoforms of ER β (ER β2, β4, and β5) can heterodimerize with ER β1 and enhance its transcriptional activity in an estradiol-dependent manner (4). ER β is expressed in a wide range of normal and malignant tissues, many of which coexpress ER α. It is proposed that ER β has an antiproliferative role, perhaps through heterodimerization with ER α and repression of its transcriptional activity at estrogen response elements (5,6). Recent studies have revealed that expression of ESR2 is subject to epigenetic regulation and that loss of ER β expression positively contributes to epithelial-mesenchymal transition and enhanced invasiveness in prostate cancer (7,8). ER β has also been found to be negatively regulated at the posttranslational level through phosphorylation of its AF-1 domain, which promotes its ubiquitin-dependent proteasomal degradation (9,10).
- Evans, R.M. (1988) Science 240, 889-95.
- Kuiper, G.G. et al. (1996) Proc Natl Acad Sci U S A 93, 5925-30.
- Moore, J.T. et al. (1998) Biochem Biophys Res Commun 247, 75-8.
- Leung, Y.K. et al. (2006) Proc Natl Acad Sci U S A 103, 13162-7.
- Hall, J.M. and McDonnell, D.P. (1999) Endocrinology 140, 5566-78.
- Pettersson, K. et al. (2000) Oncogene 19, 4970-8.
- Zhu, X. et al. (2004) Am J Pathol 164, 2003-12.
- Mak, P. et al. (2010) Cancer Cell 17, 319-32.
- Tateishi, Y. et al. (2006) Mol Cell Biol 26, 7966-76.
- Picard, N. et al. (2008) Mol Endocrinol 22, 317-30.
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