USP2 active domain (human recombinant)

Ubiquitin-specific protease 2 (USP2), also known as ubiquitin carboxyl-terminal hydrolase 2, is a cysteine protease involved in intracellular protein degradation by deubiquitinating degraded protein, including Mdm2, Mdm4, and CCND1. In both normal and cancer cells, it regulates G1/S cell-cycle transition. It may regulate p53-dependent pathways by deubiquitinating Mdm2, indirectly promoting p53 degradation and limiting its activity.. Regulated by androgen, USP2 is over-expressed in prostate cancer and stabilizes fatty acid synthase (FASN), which is associated with the malignancy of some aggressive prostate cancers. Some of these oncogenic properties may be linked to its deubiquitinating activity. One hypothesis is that USP2 may stabilize short-lived proteins that may act to induce apoptosis. USP2 has also been shown to regulate the intrinsic circadian rhythm and its capacity to respond to external cues, in a non-degradative manner by acting on the core clock component PER1. This protein is a truncation containing the active catalytic domain (residues 259-605) of USP2 and a C-terminal His-tag.Synonyms: Ubiquitin C-terminal Hydrolase 2, Ubiquitin-specific Protease 2. Purity: >95% estimated by SDS-PAGE. Source: C-terminally Histidine-tagged human USP2 enzyme (active catalytic domain) purified from E. coli. Amino Acids: 259-605 (active catalytic domain). MW: 40.9 kDa. Formulation: (Request formulation change), 50 mM HEPES, pH 8.0, 150 mM sodium chloride, 1 mM DTT, and 0.1 mM EDTA. UniProt Accession #: O75604.