产品名称
Glutaredoxin-S2, E. coli, Glutaredoxin functions as a glutathione-dependent hydrogen donor for ribonucleotide reductase.
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
Quality Level
Gene Information
Escherichia coli ... grxB(946926)
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.
Disclaimer
Toxicity: Standard Handling (A)
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.
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.
Units are defined using a standard HED assay.
Physical form
Lyophilized from 0.5% NH₄HCO₃.
Preparation Note
Reconstitute in 1 ml 50 mM Tris-HCl, 1 mM EDTA, pH 7.5 to yield a final concentration of 1 mg/ml.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
存储类别
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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
Protein S-glutathionylation and the regulation of cellular functions
Mailloux RJ, et al.
Journal of Separation Science, 217-247 (2020)
Unique thiol metabolism in trypanosomatids: Redox homeostasis and drug resistance
Ali V, et al.
Advances in Parasitology, 117, 75-155 (2022)
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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