BRD4, like other human members of the BET family of chromatin-binding proteins (BRD2, BRD3, BRDT), comprises two bromodomains, protein modules that bind epsilon-N-acetyllysine residues. The ubiquitously expressed BRD4 functions as a transcriptional regulator with roles in cell cycle progression and has recently been shown to be an atypical kinase that can phosphorylate RNA Pol II. Recent structural studies have shown that BRD4-1 (BRD4 bromomdomain 1), like the bromodomain 1 of fellow BET family protein BRDT, can bind simultaneously to two acetyllysine residues with appropriate spacing and sequence context, for example a histone H4 peptide acetylated at lysines 5 and 8 (H4K5AcK8Ac). Chromosomal translocations that produce BRD4-NUT fusion proteins are implicated in causation of a rare and aggressive cancer, NUT midline carcinoma. Selective inhibitors of BRD4/BET family bromodomains are showing promise as possible therapeutic agents for cancer and inflammation.
ACCESSION #: NM_058243
INCLUDES AMINO ACIDS: 349-460
MW: 40.1 kDa
EXPRESSION SYSTEM: E. coli
SUPPLIED AS: Solution of purified recombinant protein in 20 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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We also offer assay services for BRD4-2 (GST).