Chromatin Regulation / Acetylation

Di-Methyl Histone H3 (Lys9) Antibody

イイネ!(0) Di-Methyl Histone H3 (Lys9) Antibodyの使用例 Di-Methyl Histone H3 (Lys9) Antibody Data Sheet PDF
CSTコード 包装
希望納入価格 (円)
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2012年2月8日17時20分 現在
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下記ステップについては、データシートの右側もあわせてご参照ください。

IHC-P: 抗体希釈液 / 抗原賦活化

用途(希釈倍率)
ウェスタンブロッティング(1:1,000)、免疫沈降(1:25)、免疫組織染色(パラフィン)(1:200)、免疫蛍光細胞染色(IF-IC)(1:500)、ChIP(1:25)
種交差性
ヒト、マウス、ラット、サル、出芽酵母、キイロショウジョウバエ
特異性・感度
内在性レベルのLys9 がジメチル化されたHistone H3 タンパク質を検出します。Lys9 がメチル化されていない、モノメチル化、トリメチル化されたHistone H3 タンパク質とは交差しません。さらに、Lys27 がジメチル化、トリメチル化されたHistone H3 タンパク質とも交差しません。
検出タンパク質の分子量
17 kDa
使用抗原
Lys9 がジメチル化されたHistone H3 タンパク質のN末端領域(合成ペプチド)
抗体の由来
ウサギ
貯法
-20℃
社内データ

Western Blotting

Western Blotting

Western blot analysis of whole cell lysates from HeLa, NIH/3T3, H-4-II-E and COS cells, using Di-Methyl-Histone H3 (Lys9) Antibody.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human breast carcinoma, using Di-Methyl-Histone H3 (Lys9) Antibody.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human Non-Hodgkin's lymphoma, using Di-Methyl-Histone H3 (Lys9) Antibody.


IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human benign prostate hypertrophy (BPH), using Di-Methyl-Histone H3 (Lys9) Antibody.

IF-IC

IF-IC

Confocal immunofluorescent analysis of NIH/3T3 cells showing nuclear localization when labeled with Di-Methyl-Histone H3 (Lys9) Antibody (green). Actin filaments have been labeled with Alexa Fluor® 555 phalloidin (red).

Chromatin IP

Chromatin IP

Chromatin immunoprecipitations were performed with cross-linked chromatin from 4 x 106 HeLa cells and either 20 μl of Di-Methyl-Histone H3 (Lys9) Antibody or 2 μl 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 AFM Intron 1 Primers #5098, SimpleChIP® Human α Satellite Repeat Primers #4486, SimpleChIP® Human RPL30 Exon 3 Primers #7014, and SimpleChIP® Human GAPDH Exon 1 Primers #5516. 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.


ELISA-Peptide

ELISA-Peptide

Di-Methyl-Histone H3 (Lys9) Antibody specificity was determined by peptide ELISA. The graph depicts the binding of the antibody to pre-coated di-methyl histone H3 (Lys9) peptide in the presence of increasing concentrations of various competitor peptides. As shown, only the di-methyl histone H3 (Lys9) peptide competed away binding of the antibody.

バックグラウンド

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).

  1. Peterson, C.L. and Laniel, M.A. (2004) Curr. Biol. 14, R546-R551.
  2. Kubicek, S. et al. (2006) Ernst Schering Res. Found Workshop, 1-27.
  3. Lin, W. and Dent, S.Y. (2006) Curr. Opin. Genet. Dev. 16, 137-142.
  4. Lee, D.Y. et al. (2005) Endocr. Rev. 26, 147-170.
  5. Daniel, J.A. et al. (2005) Cell Cycle 4, 919-926.
  6. Shi, X. et al. (2006) Nature 442, 96-99.
  7. Wysocka, J. et al. (2006) Nature 442, 86-90.
  8. Wysocka, J. et al. (2005) Cell 121, 859-872.
  9. Trojer, P. and Reinberg, D. (2006) Cell 125, 213-217.
使用例
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本製品は試験研究用です。

Di-Methyl Histone H3 (Lys9) Antibody

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