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AB140732

重组人 YOD1 蛋白 (His tag N-Terminus)

Recombinant Human YOD1 protein (His tag N-Terminus)

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Recombinant Human YOD1 protein (His tag N-Terminus) 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.

查看别名

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 (His tag N-Terminus) (AB140732)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human YOD1 protein (His tag N-Terminus) (AB140732)

SDS-PAGE analysis of ab140732

SDS-PAGE - Recombinant Human YOD1 protein (His tag N-Terminus) (AB140732)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human YOD1 protein (His tag N-Terminus) (AB140732)

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

关键信息

纯度

>90% SDS-PAGE

表达系统

Escherichia coli

标签

His tag N-Terminus

应用

SDS-PAGE, Mass Spec

applications

生物活性

No

访问

Q5VVQ6

不含动物源

No

不含载体蛋白

No

种属

Human

存储溶液

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

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反应性数据

{ "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>" } } }
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序列信息

[{"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"}]}]
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性能和储存信息

运输条件
Blue Ice
推荐的短期储存时间
1-2 weeks
推荐的短期储存条件
+4°C
推荐的长期储存条件
-20°C
分装信息
Upon delivery aliquot
储存信息
Avoid freeze / thaw cycle
False
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补充信息

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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特殊说明

形式

Liquid

附加说明

ab140732 was purified using conventional chromatography techniques.

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常规信息

功能

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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产品实验方案

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靶点信息

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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