Monoubiquitylation of lysine 120 on human histone H2B is associated with transcriptional activity. The RNF20/40 complex functions as the E3 ligase and UbcH6 as the E2 conjugating enzyme to monoubiquitinate this site to stimulate HOX gene expression. Monoubiquitylation of lysine 120 increases histone chaperone FACT function resulting in transcript elongation and the generation of longer transcripts. This monoubiquitylated peptide (Ac-AVSEGTKAVTK(ubiquitin)YTSSK-NH2) can be used for deubiquitylation assays or to study ubiquitin binding domain recognition. In contrast to traditional DUB substrates, like ubiquitin-AMC and ubiquitin-rhodamine, which measure cleavage of amide bonds, utilization of a monoubiquitylated peptide as a DUB substrate measures cleavage of an isopeptide bond and allows determination of the influence of sequence proximal to the ubiquitylated lysine on specificity.
|Molecular Weight||10,244.7 Da|
|Storage||-20 °C (dry); -80°C (solution), avoid freeze/thaw cycles|