Phosphatase and TENsin homolog (PTEN) negatively regulates the phosphatidylinositol-3-kinase/AKT pathway and is one of the most frequently mutated genes in human cancer. Monoubiquitylation of PTEN at lysine 13 and lysine 289 results in increased nuclear localization of PTEN where it is implicated in phosphatase-independent functions including regulation of the activity and stability of p53. This monoubiquitylated peptide (Ac-IKEIVSRNK(ubiquitin)RRYQEDGF-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 monoubiquitinated 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. Custom monoubiquitylated peptides can be generated from the sequence of your choosing for use as DUB substrates or in ubiquitin binding studies. Various affinity tags, fluorescent labels and mutant ubiquitins are available to facilitate different assay modalities.
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