| 货号 | 4243T |
| 反应种属 | Human,Mouse,Rat,Monkey, |
| 来源宿主 | Rabbit |
| 应用 | WB |
| 目标/特异性 | Acetyl-Histone H3 (Lys56) Antibody detects endogenous levels of histone H3 only when acetylated on Lys56. This antibody does not cross-react with histone H3 acetylated on lysines 9, 14, 18 or 27. |
| 使用方法 | WB(1:1000) |
| 供应商 | CST |
| 灵敏度 | Endogenous |
| 背景 | Modulation of chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of DNA wound around eight core histone proteins (two each of H2A, H2B, H3, and H4), is the primary building block of chromatin (1). The amino-terminal tails of core histones undergo various post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (2-5). These modifications occur in response to various stimuli and have a direct effect on the accessibility of chromatin to transcription factors and, therefore, gene expression (6). In most species, histone H2B is primarily acetylated at Lys5, 12, 15, and 20 (4,7). Histone H3 is primarily acetylated at Lys9, 14, 18, 23, 27, and 56. Acetylation of H3 at Lys9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms (2,3). Phosphorylation at Ser10, Ser28, and Thr11 of histone H3 is tightly correlated with chromosome condensation during both mitosis and meiosis (8-10). Phosphorylation at Thr3 of histone H3 is highly conserved among many species and is catalyzed by the kinase haspin. Immunostaining with phospho-specific antibodies in mammalian cells reveals mitotic phosphorylation at Thr3 of H3 in prophase and its dephosphorylation during anaphase (11). |
| 存放说明 | -20C |
| 计算分子量 | 17 |
| 参考文献 | 1 . Workman, J.L. and Kingston, R.E. (1998) Annu Rev Biochem 67, 545-79. 2 . Hansen, J.C. et al. (1998) Biochemistry 37, 17637-41. 3 . Strahl, B.D. and Allis, C.D. (2000) Nature 403, 41-5. 4 . Cheung, P. et al. (2000) Cell 103, 263-71. 5 . Bernstein, B.E. and Schreiber, S.L. (2002) Chem Biol 9, 1167-73. 6 . Jaskelioff, M. and Peterson, C.L. (2003) Nat Cell Biol 5, 395-9. 7 . Thorne, A.W. et al. (1990) Eur J Biochem 193, 701-13. 8 . Hendzel, M.J. et al. (1997) Chromosoma 106, 348-60. 9 . Goto, H. et al. (1999) J Biol Chem 274, 25543-9. 10 . Preuss, U. et al. (2003) Nucleic Acids Res 31, 878-85. 11 . Dai J et al. (2005) Genes Dev 19, 472–88 12 . Chen, C.C. et al. (2008) Cell 134, 231-43. 13 . Li, Q. et al. (2008) Cell 134, 244-55. 14 . Das, C. et al. (2009) Nature 459, 113-7. 15 . Yang, B. et al. (2009) Cell Cycle 8, 2662-3. |
Confocal immunofluorescent analysis of HeLa cells, untreated (left) and TSA-treated (#9950; right), using Acetyl-Histone H3 (Lys56) Antibody (green). Actin filaments were labeled with DY-554 phalloidin (red). 使用Acetyl-Histone H3 (Lys56) Antibody (绿色)，共聚焦免疫荧光分析HeLa细胞，细胞分为untreated (左图)和TSA-treated (#9950;右图)。DY-554 phalloidin标记微丝蛋白(红色)。 | |
Acetyl-Histone H3 (Lys56) Antibody specificity was determined by peptide ELISA. The graph depicts the binding of the antibody to pre-coated acetyl-histone H3 (Lys56) peptide in the presence of increasing concentrations of various competitor peptides. As shown, only the acetyl-histone H3 (Lys56) peptide competed away binding of the antibody. 通过peptide ELISA确定Acetyl-Histone H3 (Lys56) Antibody的特异性。该图描述了抗体与提前包被的acetyl-histone H3 (Lys56) peptide的结合能力，并且多肽中含有浓度递增的不同竞争多肽。如同所示，仅acetyl-histone H3 (Lys56) peptide竞争脱离抗体的结合。 | |
Western blot analysis of extracts from HeLa, C6 and COS cells, untreated or treated with Trichostatin A (TSA) #9950 (400 nM for 18 h), using Acetyl-Histone H3 (Lys56) Antibody (upper) and Histone H3 Antibody #9715 (lower). 使用Acetyl-Histone H3 (Lys56) Antibody (上图)或Histone H3 Antibody #9715 (下图)，免疫印迹(Western blot)分析HeLa、C6和COS细胞中Acetyl-Histone H3 (Lys56)和Histone H3蛋白水平，细胞分为untreated或Trichostatin A (TSA) #9950 (400 nM for 18 h) treated。 |
