H3.3S31phos,K36me3 Recombinant Nucleosome, Biotinylated

Histone phosphorylation is a post-translational modification (PTM) wherein a phosphate group is added to a histone protein,
predominantly occurring on serine, threonine, and tyrosine residues. In combination with other PTMs, histone phosphorylation
constitutes the “histone code,” acting as a language read by proteins to regulate chromatin structure and gene expression.
Histone phosphorylation is involved in chromatin remodeling and compaction associated with diverse cellular processes,
including DNA damage repair, transcription regulation, cell division, and apoptosis [1]. Histone phosphorylation is also
observed on non-canonical histones, particularly H3.3, where it plays roles in transcriptional regulation. Recombinant
mononucleosomes containing phosphorylated histones can be used to study the biological functions of histone
phosphorylation.

H3.3S31phos,K36me3 (histone H3.3 serine 31 phosphorylation, lysine 36 trimethylation) Recombinant Nucleosome,
Biotinylated consists of 147 base pairs of DNA wrapped around an octamer of core histone proteins (two each of H2A, H2B,
H3.3, and H4) to form a nucleosome, the basic repeating unit of chromatin. The 147 bp 601 sequence, identified by Lowary
and Widom [2], has high affinity for histone octamers and is useful for nucleosome assembly. The DNA contains a 5’ biotin-
TEG group. The variant H3.3 contains a serine at position 31, one of several discrete amino acid differences compared to
canonical H3.1. H3.3S31phos,K36me3 contains phosphorylated serine at position 31 and trimethylated lysine at position 36
on histone H3.3. H3.3S31phos,K36me3 modulates stimulation-responsive gene expression in activated macrophages via
engagement of the histone methyltransferase SETD2 and ejection of the transcriptional co-repressor ZMYND11 [3].