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AB63231

Recombinant S. cerevisiae Glutaredoxin 1 protein

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(2 Publications)

Recombinant S. cerevisiae Glutaredoxin 1 protein is a Saccharomyces cerevisiae S288C Full Length protein, expressed in Escherichia coli, with >90%, suitable for FuncS.

View Alternative Names

YCL035C, YCL35C, GRX1, Glutaredoxin-1, Glutathione-dependent oxidoreductase 1

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag C-Terminus

Applications

FuncS

applications

Biologically active

Yes

Biological activity

Strongly binds to Glutathione, reduced and oxidized.

Accession

P25373

Animal free

No

Carrier free

No

Species

Saccharomyces cerevisiae S288C

Storage buffer

pH: 7.2 - 7.6 Preservative: 0.01% Sodium azide Constituents: 0.395% Tris HCl

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>Use at an assay dependent dilution.</p>" } } }
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Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P25373","tags":[{"tag":"His","terminus":"C-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue 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
True
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Supplementary information

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

Glutaredoxin 1 also known as GLRX or thioltransferase is a small protein with a mass of around 12 kDa. It functions mechanically by catalyzing the reduction of disulfide bonds in proteins using glutathione as a cofactor. This enzyme plays a critical role in maintaining the redox balance within cells. Glutaredoxin 1 is widely expressed in various tissues with particularly high levels in the liver and brain. Its ubiquitous expression highlights its importance in cellular processes requiring reduction-oxidation reactions.
Biological function summary

This enzyme acts as an important regulator in cellular redox homeostasis and defense against oxidative stress. Glutaredoxin 1 does not technically form a complex but often interacts with multiple other proteins to modulate their redox state. It is involved in the regulation of apoptosis signaling pathways and the repair of oxidatively damaged proteins. Through these actions Glutaredoxin 1 protects cells from damage and maintains proper cellular function.

Pathways

Glutaredoxin 1 participates in key processes like the regulation of the thiol-disulfide balance and the glutathione metabolism pathway. These pathways are important for cellular detoxification and antioxidant defense. It works closely with glutathione peroxidase to mitigate oxidative damage and preserves cellular integrity by ensuring reduced forms of cysteine residues on proteins. This function links Glutaredoxin 1 to other proteins such as thioredoxin which shares similar roles in oxidative stress management.

Glutaredoxin 1 plays a significant part in neurodegenerative diseases and cardiovascular disorders. Its role in managing oxidative stress links it to conditions such as Alzheimer's disease where oxidative damage is a known contributor to disease progression. The relationship between Glutaredoxin 1 and proteins like amyloid-beta prevalent in Alzheimer's further highlights its importance. In cardiovascular disorders Glutaredoxin 1 influences the function of endothelial nitric oxide synthase a protein important for vascular health suggesting its involvement in maintaining vascular function and preventing cardiovascular diseases.
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Specifications

Form

Liquid

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General info

Function

Component of the glutathione system which performs several activities such as glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity (PubMed : 11875065, PubMed : 12684511). The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. GRX1 is less active as an oxidoreductase than GRX2 (PubMed : 18992757, PubMed : 20417731, PubMed : 9571241).

Sequence similarities

Belongs to the glutaredoxin family.

Subcellular localisation

Nucleus

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Product protocols

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Target data

Component of the glutathione system which performs several activities such as glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity (PubMed : 11875065, PubMed : 12684511). The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. GRX1 is less active as an oxidoreductase than GRX2 (PubMed : 18992757, PubMed : 20417731, PubMed : 9571241).
See full target information GRX1

Additional targets

Glutaredoxin 1
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Publications (2)

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

Life sciences 223:185-193 PubMed30885522

2019

Low frequency pulsed electromagnetic field promotes differentiation of oligodendrocyte precursor cells through upregulation of miR-219-5p in vitro.

Applications

Unspecified application

Species

Unspecified reactive species

Fei Yao,Ziyu Li,Li Cheng,Liqian Zhang,Xiaowei Zha,Juehua Jing

Cell death and differentiation 16:1167-79 PubMed19373248

2009

Glutathione disulfide induces neural cell death via a 12-lipoxygenase pathway.

Applications

Unspecified application

Species

Unspecified reactive species

H-A Park,S Khanna,C Rink,S Gnyawali,S Roy,C K Sen
View all publications
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