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In 2001, C.D. Allis and colleagues described epigenetic information in the form of post-translational histone tail modifications as the 'histone code' that is generated, interpreted, and edited by proteins they coined 'writers', 'readers', and 'erasers' in response to biophysiological and environmental cues. Bromodomain proteins play an integral role in the regulation of transcription and chromatin remodeling by acting as 'readers' of acetylated histone lysine residues. The bromodomain (BRD) is the only protein domain known to specifically recognize and bind acetylated lysine residues on histone tails, although it is also known to bind to non-histone acetylated lysine targets. The bromodomain primarily functions to anchor associated protein complexes to acetylated chromatin, thus regulating its structure and transcriptional potential. Bromodomains are present in a diverse set of proteins associated with a variety of functions, including histone acetyltransferases (GCN5, PCAF), methyltransferases (MLL, ASH1L), helicases (SMARCA), transcriptional coactivators (TRIM, TAFs), nuclear scaffolding proteins (PBRM1), ATP-dependent chromatin-remodeling complex proteins and BET family proteins. Active Motif offers high quality recombinant proteins to the bromodomain sequences of many of these common bromodomain-containing proteins for use in studies of bromodomain function.
A complete list of recombinant bromodomain proteins is shown below. Click on the protein name to see complete information.
