深圳欣博盛生物科技有限公司

H3K9ac Recombinant Nucleosome, Non-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. H3K9ac (histone H3 lysine 9 acetylation) Recombinant Nucleosome, Non-Biotinylated consists of 147 base pairs of 601 sequence DNA [2] wrapped around an octamer of core histone proteins (two each of H2A, H2B, H3.2, and H4) to form a nucleosome, the basic repeating unit of chromatin. H3K9ac nucleosome contains acetylated lysine at position 9 and a Cys to Ala substitution at position 110 on histone H3.2. H3K9 is acetylated by lysine acetyltransferases (KATs) such as KAT2A (GCN5), KAT2B (PCAF), and KAT6A (MOZ), and H3K9ac is deacetylated by lysine deacetylases (KDACs) such as SIRT1 and HDAC1 [1]. H3K9ac is found at promoters of actively transcribed genes and mediates RNA polymerase II release and transition from transcription initiation to elongation by recruiting the super elongation complex (SEC) to chromatin [3]. H3K9ac is linked to metabolic regulation through repression of glycolytic genes when deacetylated by SIRT6, and altered H3K9ac patterns are associated with tau (neurofibrillary) tangles characteristic of Alzheimer’s disease [1].

Human

E. coli & synthetic DNA

Stable for six months at -80°C from date of receipt. For best results, aliquot and avoid freeze/thaws.

Dry ice.

美国

EpiCypher