| Description |
Bromodomain (BRD) is an extensive family of protein domains, originally identified in and named after the Drosophila protein Brahma. Members of BRD family share a conserved atypical left-handed four helix bundle structure, and specifically bind to epsilon-lysine acetylated proteins. It is well known that histone acetylation and methylation play a central role in epigenetics and are important for various gene transcription events, thus the acetyl-lysine binding property of BRDs make them suitable drug targets for epigenetics. Currently, there are 46 diverse human proteins containing 61 BRDs. These include histone acetyltransferases, ATP-dependent chromatin-remodeling complex proteins, and nuclear scaffold proteins. The main functions of BRDs in vivo include chromatin acetylation and deacetylation, nucleosome assembly and remodeling, and organizations of chromosome or chromatin domains.
Recombinant human BRD1 (561-668) with His tag produced in E. coli is a single, non-glycosylated polypeptide chain containing 115 amino acids. A fully biologically active molecule, BRD1 (561-668) has a molecular mass of 13.7 kDa analyzed by reducing SDS-PAGE and is obtained by proprietary chromatographic techniques at GenScript. |
