|Other Names||Ubiquitin carboxyl-terminal hydrolase 30, Deubiquitinating enzyme 30, Ubiquitin thioesterase 30, Ubiquitin-specific-processing protease 30, Ub-specific protease 30, USP30|
|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.|
|Function||Deubiquitinating enzyme tethered to the mitochondrial outer membrane that acts as a key inhibitor of mitophagy by counteracting the action of parkin (PARK2): hydrolyzes ubiquitin attached by parkin on target proteins, such as RHOT1/MIRO1 and TOMM20, thereby blocking parkin's ability to drive mitophagy (PubMed:18287522, PubMed:24896179, PubMed:25527291, PubMed:25621951). Preferentially cleaves 'Lys-6'- and 'Lys-11'- linked polyubiquitin chains, 2 types of linkage that participate to mitophagic signaling (PubMed:25621951). Does not cleave efficiently polyubiquitin phosphorylated at 'Ser-65' (PubMed:25527291). Acts as negative regulator of mitochondrial fusion by mediating deubiquitination of MFN1 and MFN2 (By similarity).|
|Cellular Location||Mitochondrion outer membrane|
|Tissue Location||Expressed in skeletal muscle, pancreas, liver and kidney.|
email@example.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
USP30, a member of the ubiquitin-specific protease family(see USP1, MIM 603478), is a novel mitochondrial deubiquitinating(DUB) enzyme (Nakamura and Hirose, 2008 [PubMed18287522]).
Nakamura, N., et al. Mol. Biol. Cell 19(5):1903-1911(2008)Quesada, V., et al. Biochem. Biophys. Res. Commun. 314(1):54-62(2004)Puente, X.S., et al. Nat. Rev. Genet. 4(7):544-558(2003)
If you have any additional inquiries please email technical services at firstname.lastname@example.org.