| 货号 | 3443T |
| 同种亚型 | Rabbit IgG |
| 反应种属 | Human,Mouse, |
| 来源宿主 | Rabbit IgG |
| 应用 | WB |
| 目标/特异性 | Phospho-HDAC4 (Ser246)/HDAC5 (Ser259)/HDAC7 (Ser155) (D27B5) Rabbit mAb detects endogenous levels of HDAC4, HDAC5 and HDAC7 proteins only when phosphorylated on Ser246, Ser259 and Ser155, respectively. |
| 使用方法 | WB(1:1000) |
| 供应商 | CST |
| 灵敏度 | Endogenous |
| 背景 | Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7). |
| 存放说明 | -20C |
| 计算分子量 | 140, 124 |
| 参考文献 | 1 . Marmorstein, R. (2001) Cell Mol Life Sci 58, 693-703. 2 . Gregory, P.D. et al. (2001) Exp Cell Res 265, 195-202. 3 . Liu, Y. et al. (2000) Mol Cell Biol 20, 5540-53. 4 . Cress, W.D. and Seto, E. (2000) J Cell Physiol 184, 1-16. 5 . Gray, S.G. and Ekström, T.J. (2001) Exp Cell Res 262, 75-83. 6 . Thiagalingam, S. et al. (2003) Ann. N.Y. Acad. Sci. 983, 84-100. 7 . Vigushin, D.M. and Coombes, R.C. (2004) Curr Cancer Drug Targets 4, 205-18. 8 . Ha CH et al. (2008) J Biol Chem 283, 14590–9 9 . Grozinger, C.M. and Schreiber, S.L. (2000) Proc Natl Acad Sci USA 97, 7835-40. 10 . Wang, A.H. et al. (2000) Mol Cell Biol 20, 6904-12. 11 . Wang, S. et al. (2008) Proc Natl Acad Sci USA 105, 7738-43. 12 . Matthews, S.A. et al. (2006) Mol Cell Biol 26, 1569-77. 13 . Parra, M. et al. (2005) J Biol Chem 280, 13762-70. 14 . McKinsey, T.A. et al. (2000) Nature 408, 106-11. |
使用Phospho-HDAC4 (Ser246)/HDAC5 (Ser259)/HDAC7 (Ser155) (D27B5) Rabbit mAb兔单抗，免疫印迹(Western blot)分析DO11.10胸腺细胞杂交瘤细胞中Phospho-HDAC4 (Ser246)/HDAC5 (Ser259)/HDAC7 (Ser155) (D27B5)的蛋白水平，细胞为untreated 或treated for 1 h with TPA (0.2 uM)和ionomycin (0.33 uM)。该抗体的磷酸化特异性通过lambda phosphatase处理细胞来确定。使用Histone Deacetylase 4 (HDAC4) Antibody #2072、Histone Deacetylase 5 (HDAC5) Antibody #2082和Histone Deacetylase 7 (HDAC7) Antibody #2882来检测HDAC的总蛋白水平。 | |
Western blot analysis of extracts from DO11.10 thymocyte hybridoma cells, either untreated or treated for 1 h with TPA (0.2 uM) and ionomycin (0.33 uM), using Phospho-HDAC4 (Ser246)/HDAC5 (Ser259)/HDAC7 (Ser155) (D27B5) Rabbit mAb. Phospho-specificity of the antibody was determined by treating cell extracts with lambda phosphatase. Total HDAC proteins were detected using Histone Deacetylase 4 (HDAC4) Antibody #2072, Histone Deacetylase 5 (HDAC5) Antibody #2082 and Histone Deacetylase 7 (HDAC7) Antibody #2882. |
