BRD2, like other human members of the BET family of chromatin-binding proteins (BRD3, BRD4, BRDT), comprises two bromodomains, protein modules that bind epsilon-N-acetyllysine residues. When overexpressed in 293 cells, BRD2, along with BRD3, binds the hyperacetylated chromatin of transcribed genes, regions enriched in acetylated histone H4 lysine-5 (H4K5Ac), H4K12Ac, H3K14Ac, but deficient in H4K16Ac and H3K9me. A single H4K5AcK12Ac peptide can bind two copies of BRD2-2 (BRD2, bromodomain 2), each interacting with one of the two acetylated lysines. In an in vitro RNA polymerase II transcription system, binding of either BRD2 or BRD3 to a chromatin template assembled with hyperacetylated histones enabled transcription through the nucleosomes. Further, BRD2 displayed histone chaperone activity, catalyzing the transfer of histone octamers from hyperacetylated oligonucleosomes to a labeled 190 bp 5s rDNA fragment. Like BRD4, BRD2 is a ubiquitously expressed transcriptional regulator and atypical protein kinase, with functions in cell cycle progression and embryogenesis. BRD2 binds preferentially to hyperacetylated histone H4 in H2A.Z-containing nucleosomes and this interaction is required for activation of androgen receptor (AR)-regulated genes in prostate cancer cells. In addition to prostate cancer, leukemia is a potential indication for specific BRD2 inhibition. BRD2 suppresses HIV transcription in latently infected cells and may therefore represent a target in therapeutic strategies involving viral reactivation.
ACCESSION #: NM_005104
INCLUDES AMINO ACIDS: 344-454
MW: 40.0 kDa
EXPRESSION SYSTEM: E. coli
SUPPLIED AS: Solution of purified recombinant protein in 50 mM Tris/HCl, pH 7.5, 150 mM NaCl, 1.0 mM TCEP, 10% glycerol (v/v)
STORAGE: -80°C, aliquot and snap-freeze after first use.
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