| 货号 | 11052-100ug |
| 描述 | The acetylation of histone lysine residues plays a crucial role in the epigenetic regulation of gene transcription. Acetylated lysine residues are recognized by a small protein domain known as a bromodomain. The acetylation of histone lysine residues plays a crucial role in the epigenetic regulation of gene transcription. Acetylated lysine residues are recognized by a small protein domain known as a bromodomain.1 These domains function in the linking of protein complexes to acetylated nucleosomes, thereby controlling chromatin structure and gene expression. The BET family of proteins, defined by tandem Bromodomains and an Extra Terminal domain, include BRD2, BRD3, BRD4, and BRDT.2 The BET proteins play a key role in many cellular processes, including inflammatory gene expression, mitosis, and viral/host interactions.3,4,5 The isolated individual or tandem bromodomains of BRD2 and BRD4 have been shown to bind acetylated histone tails, serving to couple histone acetylation marks to the transcriptional regulation of target promoters.6,7,8,9,4 Small molecule inhibitors of these interactions hold promise as useful therapeutics for human disease.10,11,12 |
| 别名 | Bromodomain containing protein 4;HUNK1;MCAP; |
| 供应商 | Cayman |
| 应用文献 | |
| 1.Mujtaba, S.,Zeng, L. and Zhou, M.M. Structure and acetyl-lysine recognition of the bromodomain. Oncogene 26, 5521-5527 (2011). 2.Florence, B. and Faller, D.V. You bet-cha: A novel family of transcriptional regulators. Frontiers in Bioscience 6, D1008-D1018 (2011). 3.Hargreaves, D.C.,Horng, T. and Medzhitov, R. Control of inducible gene expression by signal-dependent transcriptional elongation. Cell 138(1), 129-145 (2009). 4.LeRoy, G.,Rickards, B. and Flint, S.J. The double bromodomain proteins Brd2 and Brd3 couple histone acetylation to transcription. Molecular Cell 30(1), 51-60 (2008). 5.Weidner-Glunde, M.,Ottinger, M. and Schulz, T.F. WHAT do viruses BET on? Frontiers in Bioscience 15, 537-549 (2010). 6.Liu, Y.,Wang, X.,Zhang, J., et al. Structural basics and binding properties of the second bromodomain of Brd4 with acetylated histone tails. Biochem. 47, 6403-6417 (2008). 7.Day, A.,Chitsaz, F.,Abbasi, A., et al. The double bromodomain protein Brd4 binds to acetylated chromatin during interphase and mitosis. Proceedings of the National Academy of Sciences of the United States of America 100(15), 8758-8763 (2003). 8.Umehara, T.,Nakamura, Y.,Wakamori, M., et al. Structural implications for K5/K12-di-acetylated histone H4 recognition by the second bromodomain of BRD2. FEBS Letters 584(18), 3901-3908 (2010). 9.Umehara, T.,Nakamura, Y.,Jang, M.K., et al. Structural basis for acetylated histone H4 recognition by the human BRD2 bromodomain. The Journal of Biological Chemisty 2855(10), 7610-7618 (2010). 10.Filippakopoulos, P.,Qi, J.,Picaud, S., et al. Selective inhibition of BET bromodomains. Nature 468(7327), 1067-1073 (2010). 11.Hewings, D.S.,Wang, M.,Philpott, M., et al. 3,5-Dimethylisoxazoles act as acetyl-lysine-mimetic bromodomain ligands. Journal of Medicinal Chemistry 54(19), 6761-6770 (2011). 12.Chung, C.W.,Coste, H.,White, J.H., et al. Discovery and characterization of small molecule inhibitors of the BET family bromodomains. Journal of Medicinal Chemistry 54(11), 3827-3838 (2011). | |
| 运输条件 | Dry ice in continental US; may vary elsewhere |
| 存放说明 | -80 |
| 纯度 | ≥90% |
| 稳定性 | ≥ 6 months |
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