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. The cAMP response element-binding protein (CREB) binding protein (CREBBP) bromodomain has been shown to modulate the stability and function of the tumor suppressor protein p53. CREBBP bromodomain recognizes the acetylated lysine residue 382 on p53. This product contains the bromodomain region of CREBBP.
Physical form
50 mM Tris, pH 7.5, containing 500 mM sodium chloride, 5 mM β-mercaptoethanol and 5% glycerol.
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