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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] containing a 5’ biotin-TEG group. *Histone H2B contains a glutamate-to-alanine (E-to-A) substitution at positions 105 and 113 (H2BE105A,E113A). H2BE105 and H2BE113 are 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]. H2B E105 and E113 both reside in H2B alphaC extension and are associated with nucleosome binding factors such as histone H4 N-terminal tail, LANA, RCC1, HMGN2 and SMARCB1 [2,5].
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