Chromatin Regulation / Acetylation
HP1β Antibody
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イイネ!(0)
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| CSTコード |
包装 |
希望納入価格 (円) |
国内在庫  |
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| #2613S | 100 μL | 46,000 | |
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2613 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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2613:
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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HP1βタンパク質を検出します。HP1αおよび HP1γタンパク質とは交差しません。 |
| 使用抗原 | |
| ヒトのHP1βタンパク質のC末端領域 (合成ペプチド) |
| ※括弧付きの動物種は、配列が100%相同であるため反応すると推定されます。 |
Western Blotting

Western blot analysis of extracts from 293, NIH/3T3, C6 and COS cells, using HP1beta Antibody.
Heterochromatin protein 1 (HP1) is a family of heterochromatic adaptor molecules involved in both gene silencing and higher order chromatin structure (1). All three HP1 family members (α, β and γ) are primarily associated with centromeric heterochromatin; however, HP1β and γ also localize to euchromatic sites in the genome (2,3). HP1 proteins are approximately 25 kDa in size and each contains a conserved amino-terminal chromodomain, followed by a variable hinge region and a conserved carboxy-terminal chromoshadow domain. The chromodomain facilitates binding to histone H3 tri-methylated on Lys9, a histone "mark" closely associated with centromeric heterochromatin (4,5). The variable hinge region binds both RNA and DNA in a sequence-independent manner (6). The chromoshadow domain mediates the dimerization of HP1 proteins, in addition to binding multiple proteins implicated in gene silencing and heterochromatin formation, including the SUV39H histone methyltransferase, the DNMT1 and DNMT3a DNA methyltransferases and the p150 subunit of chromatin-assembly factor-1 (CAF1) (7-9). In addition to contributing to heterochromatin formation and propagation, HP1 and SUV39H are also found complexed with retinoblastoma (Rb) and E2F6 proteins, both of which function to repress euchromatic gene transcription in quiescent cells (10,11). HP1 proteins are subject to multiple types of post-translational modifications, including phosphorylation, acetylation, methylation, ubiquitination and sumoylation, suggesting multiple means of regulation (12-14).
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Maison, C. and Almouzni, G. (2004) Nat. Rev. Mol. Cell Biol. 5, 296-304.
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Minc, E. et al. (2000) Cytogenet. Cell Genet. 90, 279-284.
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Nielsen, A.L. et al. (2001) Mol. Cell 7, 729-739.
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Lachner, M. et al. (2001) Nature 410, 116-120.
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Bannister, A.J. et al. (2001) Nature 410, 120-124.
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Muchardt, C. et al. (2002) EMBO Rep. 3, 975-981.
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Yamamoto, K. and Sonoda, M. (2003) Biochem. Biophys. Res. Commun. 301, 287-292.
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Fuks, F. et al. (2003) Nucleic Acids Res. 31, 2305-2312.
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Murzina, N. et al. (1999) Mol. Cell 4, 529-540.
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Nielsen, S.J. et al. (2001) Nature 412, 561-565.
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Ogawa, H. et al. (2002) Science 296, 1132-1136.
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Minc, E. et al. (1999) Chromosoma 108, 220-234.
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Zhao, T. et al. (2001) J. Biol. Chem. 276, 9512-9518.
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Lomberk, G. et al. (2006) Nat. Cell Biol. 8, 407-415.