Nuclear Receptor Signaling
| CSTコード |
包装 |
希望納入価格 (円) |
国内在庫  |
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| #5513S | 100 μL | 46,000 | |
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Estrogen Receptor抗体製品一覧
5513 の推奨プロトコール
最適な結果を得るために：Cell Signaling Technology (CST) 社は、各製品の推奨プロトコールを使用することを強くお薦めいたします。
推奨プロトコールはCST社内試験の徹底的なバリデーションに基づいて作成されておりますので、正確かつ再現性の高い結果が得られます。
注：各製品に最適化されたプロトコールをリンクしています。
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5513:
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Western Blotting
| 用途(希釈倍率) | |
| ウェスタンブロッティング (1:1,000) |
| 特異性・感度 | |
| 内在性レベルのEstrogen Receptor βタンパク質を検出します。すべてのEstrogen Receptor βアイソフォームと交差すると予想されます。Estrogen Receptor αタンパク質とは交差しません。 |
| 検出タンパク質の分子量 | |
| 52 kDa、55 kDa、63 kDa |
| 使用抗原 | |
| ヒトのEstrogen Receptor β1 タンパク質のN末端近傍領域 (合成ペプチド) |
Western Blotting
Western blot analysis of extracts from various cell lines and tissues using Estrogen Receptor β Antibody.
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).
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Evans, R.M. (1988) Science 240, 889-95.
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Kuiper, G.G. et al. (1996) Proc Natl Acad Sci U S A 93, 5925-30.
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Moore, J.T. et al. (1998) Biochem Biophys Res Commun 247, 75-8.
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Leung, Y.K. et al. (2006) Proc Natl Acad Sci U S A 103, 13162-7.
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Hall, J.M. and McDonnell, D.P. (1999) Endocrinology 140, 5566-78.
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Pettersson, K. et al. (2000) Oncogene 19, 4970-8.
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Zhu, X. et al. (2004) Am J Pathol 164, 2003-12.
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Mak, P. et al. (2010) Cancer Cell 17, 319-32.
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Tateishi, Y. et al. (2006) Mol Cell Biol 26, 7966-76.
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Picard, N. et al. (2008) Mol Endocrinol 22, 317-30.
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