354406
Glutaredoxin-S2, E. coli
Glutaredoxin functions as a glutathione-dependent hydrogen donor for ribonucleotide reductase.
Synonym(s):
Grx1, grxA
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About This Item
UNSPSC Code:
12352202
Recommended Products
Quality Level
form
lyophilized
specific activity
≥175 μmole/min-mg (NADPH oxidized)
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
technique(s)
protein purification: suitable
NCBI accession no.
shipped in
wet ice
storage temp.
2-8°C
Gene Information
Escherichia coli ... grxB(946926)
General description
Research area: CELL SIGNALING
Glutaredoxins (GRXs) are small thiol belonging to the Thioredoxin (TRX) superfamily. Different isoforms with varied functions have been identified in E.coli namely: glutaredoxin 1, glutaredoxin 2, and glutaredoxin 3. Native glutaredoxin-S2 isolated from E. coli. Glutaredoxin functions as a glutathione-dependent hydrogen donor for ribonucleotide reductase. It is useful as a general disulfide reductant for the in vitro study of protein folding mechanisms and has been demonstrated to work in conjunction with protein disulfide isomerase to enhance refolding of scrambled RNase A and RNase T1.
Glutaredoxins (GRXs) are small thiol belonging to the Thioredoxin (TRX) superfamily. Different isoforms with varied functions have been identified in E.coli namely: glutaredoxin 1, glutaredoxin 2, and glutaredoxin 3. Native glutaredoxin-S2 isolated from E. coli. Glutaredoxin functions as a glutathione-dependent hydrogen donor for ribonucleotide reductase. It is useful as a general disulfide reductant for the in vitro study of protein folding mechanisms and has been demonstrated to work in conjunction with protein disulfide isomerase to enhance refolding of scrambled RNase A and RNase T1.
Application
Glutaredoxin-S2 has been used:
- to catalyze the reduction of S-glutathionylated cysteine residues, to facilitate the detection of protein S-glutathionylation in FFPE HLTF-/-CDX sections.
- for reduction of the protein sulfhydryl groups that were modified by glutathione for subsequent labeling and purification of glutathionylated mitochondrial proteins.
Biochem/physiol Actions
Glutaredoxins (Grxs) are a group of small redox proteins that play crucial roles in maintaining iron-sulfur metabolism and cellular redox homeostasis. These proteins function as thioltransferases , dehydroascorbate reductases, and transhydrogenases. They also participate in de-nitrosylation reactions and contribute to the conversion of cystine. Additionally, GRX2 plays a key role in neural and cardiac development. Low levels of GRX2 transcripts in humans may lead to conditions such as fibrosis, hypertrophy, and infarctions of the left ventricle.
Warning
Toxicity: Standard Handling (A)
Unit Definition
Units are defined using a standard HED assay.
Physical form
Lyophilized from 0.5% NH₄HCO₃.
Reconstitution
Reconstitute in 1 ml 50 mM Tris-HCl, 1 mM EDTA, pH 7.5 to yield a final concentration of 1 mg/ml.
Other Notes
Ruoppolo, M., et al. 1997. Biochemistry36, 12259.
Sun, C., et al. 1997. Protein Sci.6, 383.
Prinz, W.A., et al. 1997. J. Biol. Chem.272, 15661.
Holmgren, A. and Alund, F. 1995 Methods Enzymol.252, 283.
Hoog, J.O., et al. 1986. Gene43, 13.
Sun, C., et al. 1997. Protein Sci.6, 383.
Prinz, W.A., et al. 1997. J. Biol. Chem.272, 15661.
Holmgren, A. and Alund, F. 1995 Methods Enzymol.252, 283.
Hoog, J.O., et al. 1986. Gene43, 13.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Unique thiol metabolism in trypanosomatids: Redox homeostasis and drug resistance
Ali V, et al.
Advances in Parasitology, 117, 75-155 (2022)
Protein S-glutathionylation and the regulation of cellular functions
Mailloux RJ, et al.
Journal of Separation Science, 217-247 (2020)
J O Höög et al.
Gene, 43(1-2), 13-21 (1986-01-01)
Two DNA segments, together comprising 1147 bp and containing the glutaredoxin (GRX) gene, grx, from Escherichia coli K-12 were cloned and characterized in M13mp9. The gene was identified by hybridization with synthetic oligodeoxyribonucleotide probes corresponding to parts of the amino
Glutaredoxin: Discovery, redox defense and much more
Ogata F T, et al.
Redox Biology, 43, 101975-101975 (2021)
M Ruoppolo et al.
Biochemistry, 36(40), 12259-12267 (1997-10-07)
Protein folding, associated with oxidation and isomerization of disulfide bonds, was studied using reduced and denatured RNase A (rd-RNase A) and mixed disulfide between glutathione and reduced RNase A derivative (GS-RNase A) as starting materials. Folding was initiated by addition
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