Bromodomain-containing protein 4 (BRD4) belongs to the BET subclass of proteins, which are characterized by two N-terminal bromodomains and one ET (Extra Terminal) domain. BRDs associate with chromatin through their bromodomains that recognize acetylated histone lysine residues. The ET domain functions as a protein binding motif and exerts atypical serine-kinase activity. BRD4 has been identified recently as a therapeutic target in many cancers, including acute myeloid leukemia, multiple myeloma, Burkitt's lymphoma, NUT midline carcinoma, colon cancer, and breast cancer. BRD4 regulates the transcription of oncogenes, HIV, and human papilloma virus (HPV). It has been shown to bind and phosphorylate RNA POL II, which implicates its involvement in the regulation of eukaryotic transcription. Recombinant BRD4 (44-168) is suitable for use in the study of enzyme kinetics, inhibitor screening, and selectivity profiling.
