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 PBRM1 gene encodes the bromodomain-containing protein Polybromo-1D (PBRM1). PBRM1 contains six bromodomains and is a component of the SWI/SNF complex, PBAF. PBAF is targeted to acetylated sites in chromatin by the PBRM1 bromodomains, where it plays a role in cell cycle regulation and tumor suppression. This product contains the bromodomain 1 region of PBRM1.
重組人Polybromo-1D bromodomain結構域1 (23-156 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% glycerol, and 5 mM β-mercaptoethanol.
