Nucleosome, Recombinant Human, H2AK119ub1 dNuc, Biotinylated

Histone ubiquitination is a post-translational modification (PTM) wherein ubiquitin is added to a lysine residue of a histone
protein. In combination with other PTMs, histone ubiquitination constitutes the “histone code,” acting as a language read by
proteins to regulate chromatin structure and gene expression. Ubiquitin is added through the sequential actions of E1
activating, E2 conjugating, and E3 ligating enzymes and is removed by deubiquitinating enzymes (DUBs). Histone
ubiquitination plays an integral role in DNA damage response and has been implicated in transcriptional regulation and DNA
replication [1]. Recombinant nucleosomes containing ubiquitinated histones are useful to study the biological functions of
histone ubiquitination.

H2AK119ub1 (histone H2A lysine 119 ubiquitination) Recombinant Nucleosome, Biotinylated consists of 147 base pairs of
601 sequence DNA [2] wrapped around an octamer of core histone proteins (two each of H2A, H2B, H3.1, and H4) to form a
nucleosome, the basic repeating unit of chromatin. The DNA contains a 5’ biotin-TEG group. H2AK119ub1 nucleosome
contains ubiquitinated lysine at position 119 on histone H2A. H2AK119 is ubiquitinated by E3 ligase RING1A/B, subunits of
the polycomb repressive complex 1 (PRC1), in vivo. H2AK119ub1 is an abundant histone mark that plays a role in
transcriptional regulation [1].