AUS 1800 252 204
NZ 0800 448 340
Integrated Sciences is partnered with innovative and reliable brands and aims to meet the specialist needs of our customers.
EpiCypher
Mononucleosomes assembled from recombinant human histones expressed in E. coli (two each of histones H2A*, H2B, H3 and H4; accession numbers: H2A-P04908*; H2B-O60814; H3.1-P68431; H4-P62805) wrapped by 147 base pairs of 601 positioning sequence DNA [1]. *Histone H2A contains a glutamate-to-lysine (E-to-K) substitution at position 92 (H2AE92K). H2AE92 is among key residues forming a negatively charged region on the nucleosome surface named the “acidic patch”. The acidic patch is a conserved interaction hub for neighboring nucleosomes and nucleosome binding proteins, often via salt bridges with arginine anchors, and is functionally critical in chromatin condensation and chromatin remodeling [2-4]. H2AE92 resides in the H2A C-terminal extension and is associated with nucleosome binding factors such as histone H4 N-terminal tail, LANA, RCC1, IL-33, SIR3, HMGN2, and remodeling ATPases [2-4]. H2AE92K disrupts binding with SMARCB1 [5].
Follow us