| 货号 | 51198S |
| 同种亚型 | Rabbit IgG |
| 反应种属 | Human, Mouse, Rat, Monkey |
| 应用 | F |
| 目标/特异性 | Di-Methyl-Histone H3 (Lys9) (D85B4) XP® Rabbit mAb (Alexa Fluor® 488 Conjugate) detects endogenous levels of histone H3 only when di-methylated on Lys9. The antibody does not cross-react with non-methylated, mono-methylated or tri-methylated Histone H3 Lys9. In addition, the antibody does not cross-react with histone H3 di-methylated on Lys4, Lys27, or Lys36, or histone H4 di-methylated on Lys20. |
| 使用方法 | Flow Cytometry (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). |
| 存放说明 | 4C |
| 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. |
Flow cytometric analysis of HeLa cells using Di-Methyl-Histone H3 (Lys9) (D85B4) XP® Rabbit mAb (Alexa Fluor® 488 Conjugate) (green) compared to concentration-matched Rabbit (DA1E) mAb IgG XP® Isotype Control (Alexa Fluor® 488 Conjugate) #2975 (red). |
