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AB269141

Recombinant human YOD1 protein (His tag)

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(1 Publication)

Recombinant human YOD1 protein (His tag) is a Human Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.

View Alternative Names

DUBA8, HIN7, OTUD2, PRO0907, YOD1, Ubiquitin thioesterase OTU1, DUBA-8, HIV-1-induced protease 7, OTU domain-containing protein 2, HIN-7, HsHIN7

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SDS-PAGE - Recombinant human YOD1 protein (His tag) (AB269141)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human YOD1 protein (His tag) (AB269141)

SDS-PAGE analysis of ab269141.

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q5VVQ6

Animal free

No

Carrier free

No

Species

Human

Storage buffer

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

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q5VVQ6","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

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.
Biological function summary

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.

Pathways

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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Specifications

Form

Liquid

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General info

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).

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Product protocols

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Target data

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).
See full target information YOD1
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Cell death & disease 16:334 PubMed40274778

2025

The deubiquitinase YOD1 suppresses tumor progression by stabilizing ZNF24 in clear cell renal carcinoma.

Applications

Unspecified application

Species

Unspecified reactive species

Ji Liu,Ying Lu,Runye Zhu,Ping Xi,Zhihao Yang,Zhipeng Zhang,Yunbing Xiong,Yifu Liu,Qiqi Zhu,Ting Sun,Wenjie Xie,Binbin Gong
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Product promise

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