Nucleosome, Recombinant Human, H4 Tetraacetyl (H4K5,8,12,16ac) dNuc, Biotinylated

Histone acetylation is a post-translational modification (PTM) wherein an acetyl group is added to a lysine residue of a histone protein. In combination with other PTMs, histone acetylation constitutes the “histone code,” acting as a language read by proteins to regulate chromatin structure and gene expression. Histone acetylation is associated with gene activation and binds reader proteins such as SWI/SNF (BAF) chromatin remodeling complexes, BRD4, and TAF1 [1]. Recombinant nucleosomes containing acetylated histones are useful to study the biological functions of histone acetylation. 

Nucleosome, Recombinant Human, H4 Tetraacetyl (H4K5,8,12,16ac) dNuc, Biotinylated consists of 147 base pairs of 601 sequence DNA [2] wrapped around an octamer of core histone proteins (two each of H2A, H2B, H3.1, and H4) to form a
nucleosome, the basic repeating unit of chromatin. The DNA contains a 5’ biotin-TEG group. H4 Tetraacetyl nucleosome contains histone H4 with N-terminal α-acetylation and acetylated lysine at positions 5, 8, 12 and 16.