Recombinant BRPF1 protein (His tag)

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Introducing the recombinant Peregrin (BRPF1) Bromodomain Fragment (residues 488-749), a high-purity protein tool designed for investigating bromodomain-mediated histone recognition and acetyltransferase complex assembly. This 262-amino acid fragment retains the complete bromodomain (residues 628-732), making it an ideal reagent for epigenetic research, structural studies, and screening applications targeting histone-binding modules.

Peregrin (BRPF1) is a critical scaffold subunit in multiple histone acetyltransferase (HAT) complexes, including MOZ/MORF and HBO1 complexes, which exhibit histone H3 acetyltransferase activity. It plays a key regulatory role by directing KAT7/HBO1 specificity toward histone H3 Lys-14 acetylation (H3K14ac), while some complexes preferentially mediate H3 Lys-23 acetylation (H3K23ac). BRPF1 positively regulates transcription factors RUNX1 and RUNX2 and localizes primarily to the nucleus and chromosomes, particularly at transcription start sites, with additional presence in the cytoplasm. Its nuclear localization depends on interaction partners KAT6A, ING5, and MEAF6, positioning it as a central regulator of chromatin modification and gene expression processes.