| 货号 | 11649-100ug |
| 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.1 These domains function in the linking of protein complexes to acetylated nucleosomes, thereby controlling chromatin structure and gene expression. Thus, bromodomains serve as “readers” of histone acetylation marks regulating the transcription of target promoters.2 Bromodomain testis specific (BRDT) shares homology with the RING3 protein. The two bromodomains of BRDT recognize acetylated histone H4. Loss of BRDT leads to defects in spermatogenesis.3 In addition to testis specific expression, BRDT was found in approximately 20% of non-small cell lung cancers.4 |
| 别名 | BRD6;Bromodomain testis-specific protein;Cancer/testis antigen 9;CT9;RING3-like protein; |
| 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.Muller, S.,Filippakopoulos, P., and Knapp, S. Bromodomains as therapeutic targets. Expert Rev.Mol.Med. 13, 1-21 (2011). 3.Barda, S.,Paz, G.,Yogev, L., et al. Expression of BET genes in testis of men with different spermatogenic impairments. Fertil.Steril. 97(1), 46-52 (2012). 4.Scanlan, M.J.,Altorki, N.K.,Gure, A.O., et al. Expression of cancer-testis antigens in lung cancer: Definition of bromodomain testis-specific gene (BRDT) as a new CT gene, CT9. Cancer Letters 150(2), 155-164 (2000). | |
| 运输条件 | Dry ice in continental US; may vary elsewhere |
| 存放说明 | -80 |
| 纯度 | ≥95% |
| 稳定性 | ≥ 1 year |
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