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. TRIM24 is a transcriptional cofactor, whose inactivation leads to hepatocellular carcinoma in mice. The N-terminal TRIM domain of TRIM24 binds ligand-bound nuclear receptors, while its tandem C-terminal plant homeo-domain and bromodomain target TRIM24 to acetylated histones in chromatin. This product contains the bromodomain region of TRIM24.||Source:|Recombinant protein corresponding to aa896-1014 from the bromodomain region of human TRIM24, fused to GST-tag at N-terminal, expressed in E. coli. ||Molecular Weight: |~40.9kD (aa896-1014 + NT GST Tag)||Storage and Stability:|Aliquot to avoid repeated freezing and thawing and store at -70°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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