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 Technical Information Synonyms BRD6 Bromodomain testis-specific protein Cancer/testis antigen 9 CT9 RING3-like protein Purity 90% Source recombinant N-terminal GST-tagged protein expressed in E. coli MW 41.2 kDa Formulation 50 mM Tris, pH 7.5, containing 500 mM sodium chloride, 5% glycerol and 5 mM -mercaptoethanol