Recombinant human YOD1 protein (His tag) is a Human Full Length protein, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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).
DUBA8, HIN7, OTUD2, PRO0907, YOD1, Ubiquitin thioesterase OTU1, DUBA-8, HIV-1-induced protease 7, OTU domain-containing protein 2, HIN-7, HsHIN7
Recombinant human YOD1 protein (His tag) is a Human Full Length protein, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
pH: 7
Preservative: 1.02% Imidazole
Constituents: 25% Glycerol (glycerin, glycerine), 1.74% Sodium chloride, 0.82% Sodium phosphate, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.002% PMSF
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).
YOD1 also known as OTUD1 is a deubiquitinating enzyme from the ovarian tumor domain family. It possesses a molecular mass of approximately 48 kDa. Mechanically YOD1 removes ubiquitin from protein substrates a step critical for regulating protein fate and function within the cell. Expression of YOD1 is found in various tissues but appears highly expressed in the brain and liver. Its enzymatic activity depends on recognizing and cleaving ubiquitin from polyubiquitin chains which impacts cellular processes like protein degradation and trafficking.
YOD1 plays a fundamental role in modulating the ubiquitin-proteasome system participating in controlling protein quality and turnover. It acts as part of larger ubiquitin-editing complexes and influences the stability and degradation of proteins like misfolded or damaged proteins. Misfunction in these processes can lead to impaired cellular homeostasis. YOD1 can contribute to the regulation of the endoplasmic reticulum-associated degradation (ERAD) pathway ensuring proteins are adequately processed and degraded when necessary.
YOD1 is integral in the ubiquitin-proteasome and endoplasmic reticulum-associated degradation pathways. These pathways are important for maintaining proteostasis by removing aberrant proteins. YOD1 is closely related to other deubiquitinating enzymes such as USP7 which together help regulate protein degradation. YOD1's activity impacts pathways that control cellular stress responses and protein quality maintenance highlighting its involvement in cellular health and function.
Improper YOD1 function appears linked to neurodegenerative diseases and cancer. In neurodegenerative diseases like Alzheimer's YOD1 contributes to the removal of protein aggregates and stress response management. Related proteins such as USP7 also partake in these processes providing redundancy and complexity in the protein degradation systems. In cancer pathways involving YOD1 could influence cell proliferation and survival making it a subject of interest for therapeutic targets.
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SDS-PAGE analysis of ab269141.
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