General description

The acetylation of histone lysine residues plays a crucial role in the epigenetic regulation of gene transcription. A bromodomain is a protein domain that recognizes acetylated lysine residues such as those on the N-terminal tails of histones. This recognition is often a prerequisite for protein-histone association and chromatin remodeling. These domains function in the linking of protein complexes to acetylated nucleosomes, thereby controlling chromatin structure and gene expression. Thus, bromodomains serve as “readers” of histone acetylation marks regulating the transcription of target promoters. BPTF is the largest component of the NURF chromatin remodeling complex. It includes adjacent PHD and bromodomains which recognize trimethylation of H3K4 or acetylation of lysines in histone 4, respectively. BPTF is an essential regulator of gene expression in early mouse embryos, and its knock-out is embryonic lethal. Duplication of the BPTF gene has been suggested to increase proliferation of cultured cancer cells, and aberrant BPTF copy numbers were found in 42% of the “NCI-60” panel of 60 human cancer cell lines. This protein product contains the bromodomain of BPTF.

Physical form

50 mM Tris, pH 7.5, containing 500 mM sodium chloride, 5 mM β-mercaptoethanol and 5% glycerol.