Glutaredoxin-1 human

Glutaredoxin-1, found in the cytosol, supplies ribonucleotide reductase with electrons and involved in general disulfide-dithiol exchanges, dehydroascorbate reduction, cellular differentiation, regulation of transcription factors, and apoptosis.

Glutaredoxins (GRXs) participate in thio-disulfide exchange reactions in the presence of GSH, NADPH, and glutathione reductase. Glutaredoxins and thioredoxins belong to related families of low molecular mass enzymes that catalyze thio-disulfide exchange reactions. These enzymes are involved in electron transport, formation of disulfide linkage, protein folding, and protein regulation by thiol redox control.
Two Glutaredoxins have been identified in mammals:

• GRX1: found in the cytosol, supplies ribonucleotide reductase with electrons and is involved in general disulfide-dithiol exchanges, dehydroascorbate reduction, cellular differentiation, regulation of transcription factors and apoptosis.
• GRX2: plays a role in the cellular response to apoptotic stimuli and oxidative stress at the mitochondrial checkpoint. GRX2 has two isoforms (GRX2a and GRX2b) derived from alternative first exons. GRX2a is targeted to mitochondria, whereas GRX2b is predicted to be localized in the nucleus. Unlike GRX1, GRX2 is not inhibited by oxidation of structural Cys residues. In addition, GRX2 can receive electrons not only from GSH, but also from thioredoxin reductase supporting both monothiol and dithiol reactions.

Supplied as lyophilized powder containing Glutaredoxin-1 (2 mg/ml), 10 mM MES buffer, 100 mM NaCl, and 1 mM DTT, 1 mM EDTA.

Reconstitute with 125 μL of 50% glycerol. The reconstituted product contains 2 mgP/mL in 10 mM MES, pH 6, 100 mM NaCl, 1 mM glutathione, and 50% glycerol.

1 unit oxidizes 1 μmole of NADPH per minute at pH 8 at 25 °C in a coupled reaction with glutathione reductase.