H3T3phos, 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]. Recombinant mononucleosomes
containing phosphorylated histones can be used to study the biological functions of histone phosphorylation.

H3T3phos (histone H3 threonine 3 phosphorylation) Recombinant Nucleosome, Biotinylated consists of 147 base pairs of
DNA 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. 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. H3T3phos nucleosome contains
phosphorylated threonine at position 3 on histone H3.2 and a Cys to Ala substitution at position 110. H3T3 is phosphorylated
during mitosis by Haspin, a mitotic chromatin-associated kinase, and becomes highly enriched at inner centromeric regions
during prometaphase and metaphase. H3T3phos is associated with chromatin segregation and binds to Survivin, a subunit of
Chromosomal Passenger Complex (CPC), to recruit CPC to the centromere during mitosis [1].