BRD7 bromodomain (human, recombinant)

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. These domains function in linking 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. BRD7 is a subunit of the polybromo-associated BRG1-associated factor (PBAF)-specific component of the switch/sucrose non-fermentable chromatin-remodeling complex. It has a tumor suppressor role by acting as a cofactor for p53 and regulating breast cancer tumorigenicity. Cells lacking BRD7 have reduced breast cancer type 1-dependent estrogen receptor alpha expression. Down-regulation of BRD7 has been demonstrated in nasopharyngeal carcinoma cell lines and in colorectal cancer. BRD7 is also involved in transcriptional gene silencing through binding to protein arginine methyltransferase 5 and polycomb repressive complex 2. This protein product contains the bromodomain region of BRD7.Synonyms: Bromodomain containing protein 7, Protein CELTIX-1. Purity: >70% estimated by SDS-PAGE. Source: recombinant N-terminal GST-tagged protein expressed in E. coli. Amino Acids: 129-252 (partial protein). MW: 42.2 kDa. Formulation: (Request formulation change), 50 mM Tris, pH 8.0, with 150 mM sodium chloride and 20% glycerol.