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. Bromodomain and PHD finger containing 3 (BRPF3) is a component of the MOZ/MORF histone acetyltransferase (HAT) complex. The addition of BRPF proteins to MOZ/MORF increases its HAT activity.3 Consequently, BRPF3 is likely to play a role in regulation of transcriptional activation by MOZ/MORF. This product contains the first bromodomain of BRPF3.
重組人BRPF3 bromodomain結構域(576-701 aa) (帶GST標簽)產品為液體即用型，其溶液組成為：50 mM Tris, pH 7.5, containing 500 mM sodium chloride, 5 mM β-mercaptoethanol and 5% glycerol.
