Chromatin Regulation / Acetylation
Tri-Methyl-Histone H3 (Lys36) (D5A7) XP® Rabbit mAb
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| CSTコード |
包装 |
希望納入価格 (円) |
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| #4909S | 100 μL | 57,000 | |
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| #4909P | 40 μL for Custom Sampler Kit |  Custom Antibody Sampler Kitの構成品を選択できます。
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シグナル伝達研究応援キャンペーン プレゼント *Pサイズのみ
Histone H3抗体製品一覧
4909 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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4909:
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ChIP Agarose
ChIP Magnetic
Western Blotting
| 用途 (希釈倍率) | |
| ウェスタンブロッティング (1:1,000)、ChIP (1:50) |
| 種交差性 | |
| ヒト、マウス、ラット、サル、(ニワトリ、ハムスター、ウシ、キイロショウジョウバエ、アフリカツメガエル、ゼブラフィッシュ) |
| 特異性・感度 | |
| 内在性レベルのLys36 がトリメチル化されたHistone H3 タンパク質を検出します。Lys36 がメチル化されていない、モノ、あるいはジメチル化されたHistone H3 タンパク質とは交差しません。また、Lys4、Lys9、Lys27 がメチル化されたHistone H3 タンパク質やLys20 がメチル化されたHistone H4 タンパク質とも交差しません。 |
| 使用抗原 | |
| Lys36 がトリメチル化されたHistone H3 タンパク質のN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 various cell lines using Tri-Methyl-Histone H3 (Lys36) (D5A7) XP® Rabbit mAb.
ELISA

Tri-Methyl Histone H3 (Lys36) (D5A7) XP® Rabbit mAb specificity was determined by peptide ELISA. The graph depicts the binding of the antibody to pre-coated tri-methyl histone H3 (Lys36) peptide in the presence of increasing concentrations of various competitor peptides. As shown, only the tri-methyl histone H3 (Lys36) peptide competed away binding of the antibody.
Chromatin IP

Chromatin immunoprecipitations were performed with cross-linked chromatin from 4 x 106 HeLa cells and either 10 μl of Tri-Methyl-Histone H3 (Lys36) (D5A7) XP® Rabbit mAb or 2 μl of Normal Rabbit IgG #2729 using SimpleChIP® Enzymatic Chromatin IP Kit (Magnetic Beads) #9003. The enriched DNA was quantified by real-time PCR using SimpleChIP® Human γ-Actin Promoter Primers #5037, SimpleChIP® Human γ-Actin Intron 3 Primers #5047, SimpleChIP® Human GAPDH Promoter Primers #4471, and SimpleChIP® Human GAPDH Intron 2 Primers #4478. The amount of immunoprecipitated DNA in each sample is represented as signal relative to the total amount of input chromatin, which is equivalent to one.
The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. Originally thought to function as a static scaffold for DNA packaging, histones have now been shown to be dynamic proteins, undergoing multiple types of post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (1). Histone methylation is a major determinant for the formation of active and inactive regions of the genome and is crucial for the proper programming of the genome during development (2,3). Arginine methylation of histones H3 (Arg2, 17, 26) and H4 (Arg3) promotes transcriptional activation and is mediated by a family of protein arginine methyltransferases (PRMTs), including the co-activators PRMT1 and CARM1 (PRMT4) (4). In contrast, a more diverse set of histone lysine methyltransferases has been identified, all but one of which contain a conserved catalytic SET domain originally identified in the Drosophila Su(var)3-9, Enhancer of zeste, and Trithorax proteins. Lysine methylation occurs primarily on histones H3 (Lys4, 9, 27, 36, 79) and H4 (Lys20) and has been implicated in both transcriptional activation and silencing (4). Methylation of these lysine residues coordinates the recruitment of chromatin modifying enzymes containing methyl-lysine binding modules such as chromodomains (HP1, PRC1), PHD fingers (BPTF, ING2), tudor domains (53BP1), and WD-40 domains (WDR5) (5-8). The discovery of histone demethylases such as PADI4, LSD1, JMJD1, JMJD2, and JHDM1 has shown that methylation is a reversible epigenetic marker (9).
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Peterson, C.L. and Laniel, M.A. (2004) Curr. Biol. 14, R546-R551.
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Kubicek, S. et al. (2006) Ernst Schering Res. Found Workshop, 1-27.
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Lin, W. and Dent, S.Y. (2006) Curr. Opin. Genet. Dev. 16, 137-142.
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Lee, D.Y. et al. (2005) Endocr. Rev. 26, 147-170.
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Daniel, J.A. et al. (2005) Cell Cycle 4, 919-926.
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Shi, X. et al. (2006) Nature 442, 96-99.
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Wysocka, J. et al. (2006) Nature 442, 86-90.
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Wysocka, J. et al. (2005) Cell 121, 859-872.
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Trojer, P. and Reinberg, D. (2006) Cell 125, 213-217.