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AB95471

Recombinant Human GRX2 protein

Recombinant Human GRX2 protein

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(1 Publication)

Recombinant Human GRX2 protein is a Human Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.

別名を表示する

GRX2, CGI-133, GLRX2

1 Images
SDS-PAGE - Recombinant Human GRX2 protein (AB95471)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human GRX2 protein (AB95471)

15% SDS-PAGE analysis of 3μg ab95471.

Key facts

精製度

>90% SDS-PAGE

発現系

Escherichia coli

タグ

His tag C-Terminus

アプリケーション

SDS-PAGE, Mass Spec

applications

生物活性

No

アクセッション番号

Q9NS18

アニマルフリー

No

キャリアフリー

No

Human

バッファー組成

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.316% Tris HCl, 0.00174% PMSF

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>" } } }

製品の詳細

This product was previously labelled as Glutaredoxin 2.

配列情報

[{"sequence":"MSAGWLDRAAGAAGAAAAAASGMESNTSSSLENLATAPVNQIQETISDNCVVIFSKTSCSYCTMAKKLFHDMNVNYKVVELDLLEYGNQFQDALYKMTGERTVPRIFVNGTFIGGATDTHRLHKEGKLLPLVHQCYLKKSKRKEFQLEHHHHHH","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q9NS18","tags":[{"tag":"His","terminus":"C-Terminus"}]}]

出荷温度及び保存条件

出荷温度
Blue Ice
短期保存温度
-20°C
長期保存温度
-20°C
分注に関する情報
Upon delivery aliquot
保管に関する情報
Avoid freeze / thaw cycle
False

補足情報

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

The target GRX2 also commonly known as GLRX2 is a human protein encoded by the GLRX2 gene. GRX2 functions as a glutaredoxin a type of enzyme involved in the process of reducing disulfide bonds in proteins which is essential for cell redox regulation. The protein has a molecular mass of approximately 16 kDa and primarily resides in the mitochondria and cytoplasm of cells. Its expression occurs in various tissues with significant levels in the heart brain and skeletal muscle indicating its broad functional roles across different organ systems.
Biological function summary

The GRX2 protein plays a critical role in maintaining cellular redox balance by facilitating the reversible oxidation of protein cysteines. This is important for protecting cells against oxidative stress. GRX2 does not function as an isolated entity but instead forms part of larger multi-protein complexes interacting with other enzymes to regulate cellular homeostasis. These interactions help to protect cells from oxidative damage promote protein folding and regenerate other antioxidants.

Pathways

GRX2 holds a significant position in the redox regulation and antioxidant pathways. It partners with thioredoxin reductase and glutathione systems to mediate these pathways and manage cellular oxidative stress. The protein's activity is closely tied to glutathione with GRX2 often acting in synergy with glutathione to reduce complex oxidized protein thiols. This collaboration is vital in the oxidative stress response where the pathway elements must efficiently counterbalance oxidative challenges.

GRX2's function links it to several oxidative stress-related conditions including neurodegenerative diseases and cardiovascular disorders. In neurodegenerative diseases like Parkinson's disease GRX2's ability to combat oxidative stress is compromised leading to neuronal damage. Additionally the protein's interaction with other redox regulatory proteins such as thioredoxin suggests interconnected roles in the progression of these disorders. Cardiovascular diseases also involve GRX2 due to its essential function in maintaining cardiovascular integrity under environmental and metabolic oxidative stress.

製品の性状

製品の状態

Liquid

補足情報

ab95471 was purified by using conventional chromatography.

一般的な情報

機能

Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.

配列の類似性

Belongs to the glutaredoxin family.

細胞内局在性

Mitochondrion

製品プロトコール

ターゲットの情報

Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.
See full target information GLRX2

文献 (1)

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

Cell chemical biology 26:366-377.e12 PubMed30661989

2019

Frenolicin B Targets Peroxiredoxin 1 and Glutaredoxin 3 to Trigger ROS/4E-BP1-Mediated Antitumor Effects.

Applications

Unspecified application

Species

Unspecified reactive species

Qing Ye,Yinan Zhang,Yanan Cao,Xiachang Wang,Yubin Guo,Jing Chen,Jamie Horn,Larissa V Ponomareva,Luksana Chaiswing,Khaled A Shaaban,Qiou Wei,Bradley D Anderson,Daret K St Clair,Haining Zhu,Markos Leggas,Jon S Thorson,Qing-Bai She
View all publications

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