Glutaredoxin-S2, E. coli

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.

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.

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.

Toxicity: Standard Handling (A)

Units are defined using a standard HED assay.

Lyophilized from 0.5% NH₄HCO₃.

Reconstitute in 1 ml 50 mM Tris-HCl, 1 mM EDTA, pH 7.5 to yield a final concentration of 1 mg/ml.

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