Otubain-1 belongs to the ovarian tumor (OTU) domain class of cysteine protease deubiquitinating enzymes and has been implicated in mediating lymphocyte antigen responsiveness and may be generally involved in RNA processing and cell adhesion/morphology. Human otubain-1 has been shown to exhibit high linkage-specificity in vitro, cleaving Lys48 (K48)-linked polyubiquitin but not K63-, K29-, K6-, or K11-linked polyubiquitin, or linear α-linked polyubiquitin. Cleavage is not limited to either end of a polyubiquitin chain, and both free and substrate-linked polyubiquitin are disassembled.
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Regulatory Status |
RUO – Research Use Only |
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