Recombinant BRD4 protein (His tag)

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Recombinant Human BRD4 Bromodomain 1 Fragment (residues 43-173) is a high-purity protein product designed for chromatin biology and epigenetic research. This 131-amino acid fragment fully encompasses the functional Bromo 1 domain of Bromodomain-containing protein 4, providing an essential tool for studying histone recognition, chromatin remodeling, and transcriptional regulation mechanisms.

Bromodomain-containing protein 4 (BRD4) is a crucial chromatin reader protein in humans that recognizes and binds acetylated histones, playing a fundamental role in epigenetic memory transmission across cell divisions and transcription regulation. The full-length protein remains associated with acetylated chromatin throughout the cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status. BRD4 localizes to the nucleus and chromosomes, where it regulates signal-inducible gene transcription by associating with the P-TEFb complex and recruiting it to promoters and enhancers. It also plays roles in displacing negative regulators from P-TEFb, transforming it into an active form that phosphorylates the C-terminal domain of RNA polymerase II. Additionally, BRD4 regulates NF-kappa-B activation through binding acetylated RELA and modulates p53/TP53-mediated transcription. The protein's specific localization to mitotic chromosomes and release upon histone deacetylation underscores its dynamic role in chromatin organization and gene expression control.