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
Quality Level
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.
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.
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.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Toxicity: Standard Handling (A)
存储类别
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Glutaredoxin.
A Holmgren et al.
Methods in enzymology, 252, 283-292 (1995-01-01)
W A Prinz et al.
The Journal of biological chemistry, 272(25), 15661-15667 (1997-06-20)
In Escherichia coli, two pathways use NADPH to reduce disulfide bonds that form in some cytoplasmic enzymes during catalysis: the thioredoxin system, which consists of thioredoxin reductase and thioredoxin, and the glutaredoxin system, composed of glutathione reductase, glutathione, and three
Iron?Sulphur Clusters, Their Biosynthesis, and Biological Functions in Protozoan Parasites
Ali V and Nozaki T
Advances in Parasitology, 83, 1-92 (2013)
C Sun et al.
Protein science : a publication of the Protein Society, 6(2), 383-390 (1997-02-01)
Human glutaredoxin is a member of the glutaredoxin family, which is characterized by a glutathione binding site and a redox-active dithiol/disulfide in the active site. Unlike Escherichia coli glutaredoxin-1, this protein has additional cysteine residues that have been suggested to
Modulation of the specific glutathionylation of mitochondrial proteins in the yeast Saccharomyces cerevisiae under basal and stress conditions
Gergondey R, et al.
The Biochemical Journal, 474(7), 1175-1193 (2017)
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