Cayman Usp2 Active Domain (Human Recombinant); Purity- Greater Th

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.

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