| 货号 | 14111T |
| 同种亚型 | Rabbit IgG |
| 反应种属 | Human,Mouse,Rat,Monkey, |
| 来源宿主 | Rabbit IgG |
| 应用 | WB, IP , IF-IC , ChIP |
| 目标/特异性 | Mono-Methyl-Histone H3 (Lys36) (D9J1D) Rabbit mAb recognizes endogenous levels of histone H3 only when mono-methylated at Lys36. The antibody does not cross-react with non-methylated, di-methylated, or tri-methylated Lys36. In addition, the antibody does not cross-react with mono-methylated histone H3 Lys4, Lys9, Lys27, or Lys79. |
| 使用方法 | WB(1:1000) IP (1:50) IF-IC (1:1600) ChIP (1:50) |
| 供应商 | CST |
| 灵敏度 | Endogenous |
| 背景 | 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). |
| 运输条件 | 1 |
| 存放说明 | -20C |
| 计算分子量 | 17 |
| 参考文献 | 1 . Peterson, C.L. and Laniel, M.A. (2004) Curr Biol 14, R546-51. 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, 137-42. 4 . Lee, D.Y. et al. (2005) Endocr Rev 26, 147-70. 5 . Daniel, J.A. et al. (2005) Cell Cycle 4, 919-26. 6 . Shi, X. et al. (2006) Nature 442, 96-9. 7 . Wysocka, J. et al. (2006) Nature 442, 86-90. 8 . Wysocka, J. et al. (2005) Cell 121, 859-72. 9 . Trojer, P. and Reinberg, D. (2006) Cell 125, 213-7. |
Western blot analysis of extracts from various cell lines using Mono-Methyl-Histone H3 (Lys36) (D9J1D) Rabbit mAb. | |
Antibody specificity was determined by western blotting. HeLa and NIH/3T3 cell extracts were probed with Mono-Methyl-Histone H3 (Lys36) (D9J1D) Rabbit mAb alone (A) or Mono-Methyl-Histone H3 (Lys36) (D9J1D) Rabbit mAb | |
pre-adsorbed with 1.5 μM of various competitor peptides (B-I). As shown, only the mono-methyl-histone H3 (Lys36) | |
peptide competed away binding of the antibody (C). |
