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YOD1 Antibody (C-term) Blocking peptide

Synthetic peptide

     
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Product Information
Primary Accession Q5VVQ6
Clone Names 100126177
Additional Information
Gene ID 55432
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 Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name YOD1
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.
Research Areas
Citations (0)
citation

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Background

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].

References

Ernst, R., et al. Mol. Cell 36(1):28-38(2009)

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$ 277.78
Cat# BP11304b
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