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AB140732

Recombinant Human YOD1 protein

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Recombinant Human YOD1 protein is a Human Full Length protein, in the 1 to 348 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.

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

2 Images
SDS-PAGE - Recombinant Human YOD1 protein (AB140732)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human YOD1 protein (AB140732)

15% SDS-PAGE analysis of ab140732 (3μg).

SDS-PAGE - Recombinant Human YOD1 protein (AB140732)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human YOD1 protein (AB140732)

SDS-PAGE analysis of ab140732

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

Q5VVQ6

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 30% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

Reactivity data

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

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMGSMFGPAKGRHFGVHPAPGFPGGVSQQAAGTKAGPAGAWPVGSRTDTMWRLRCKAKDGTHVLQGLSSRTRVRELQGQIAAITGIAPGGQRILVGYPPECLDLSNGDTILEDLPIQSGDMLIIEEDQTRPRSSPAFTKRGASSYVRETLPVLTRTVVPADNSCLFTSVYYVVEGGVLNPACAPEMRRLIAQIVASDPDFYSEAILGKTNQEYCDWIKRDDTWGGAIEISILSKFYQCEICVVDTQTVRIDRFGEDAGYTKRVLLIYDGIHYDPLQRNFPDPDTPPLTIFSSNDDIVLVQALELADEARRRRQFTDVNRFTLRCMVCQKGLTGQAEAREHAKETGHTNFGEV","proteinLength":"Full Length","predictedMolecularWeight":"40.7 kDa","actualMolecularWeight":null,"aminoAcidEnd":348,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q5VVQ6","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

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.

Specifications

Form

Liquid

Additional notes

ab140732 was purified using conventional chromatography techniques.

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).

Product protocols

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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