|Other Names||Ubiquitin thioesterase OTU1, DUBA-8, HIV-1-induced protease 7, HIN-7, HsHIN7, OTU domain-containing protein 2, YOD1, DUBA8, HIN7, OTUD2|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Synonyms||DUBA8, HIN7, OTUD2|
|Function||Hydrolase that can remove conjugated ubiquitin from proteins and participates in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by triming the ubiquitin chain on the associated substrate to facilitate their threading through the VCP/p97 pore. Ubiquitin moieties on substrates may present a steric impediment to the threading process when the substrate is transferred to the VCP pore and threaded through VCP's axial channel. Mediates deubiquitination of 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitin chains. Also able to hydrolyze 'Lys-11'-linked ubiquitin chains. Cleaves both polyubiquitin and di-ubiquitin. May play a role in macroautophagy, regulating for instance the clearance of damaged lysosomes. May recruit PLAA, UBXN6 and VCP to damaged lysosome membranes decorated with K48-linked ubiquitin chains and remove these chains allowing autophagosome formation (PubMed:27753622).|
|Cellular Location||Cytoplasm. Note=Recruited to damaged lysosomes decorated with K48-linked ubiquitin chains.|
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Provided below are standard protocols that you may find useful for product applications.
Deubiquitinating enzymes (DUBs; see MIM 603478) areproteases that specifically cleave ubiquitin (MIM 191339) linkages,negating the action of ubiquitin ligases. DUBA8 belongs to a DUBsubfamily characterized by an ovarian tumor (OTU) domain.[suppliedby OMIM].
Ernst, R., et al. Mol. Cell 36(1):28-38(2009)
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