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Glutaredoxin 1, Recombinant, Human (Glutaredoxin-1, GLRX, GRX, GRX1, MGC117407, Thioltransferase-1, TTase-1)

Cat no: G5011-01

Glutaredoxin 1, Recombinant, Human (Glutaredoxin-1, GLRX, GRX, GRX1, MGC117407, Thioltransferase-1, TTase-1)

Glutaredoxin (Grx), also known as thiol transferase, is a small heat-stable oxidoreductase. Grxs form part of the glutaredoxin system, comprising NADPH, GSH and glutathione reductase, which transfers electrons from NADPH to glutaredoxins via GSH (1). First discovered in E.coli as GSH-dependent hydrogen donors for ribonucleotide reductase, Grx catalyzes GSH-disulfide oxidoreductase via two redox-active cysteine residues (2). The active sequence (Cys-Pro-Tyr-Cys) is conserved in a variety of species. The 12kD dithiol protein has a role in reduction of mixed disulfides in cells exposed to oxidative stress (3).\n\nSource:\nRecombinant corresponding to aa1-106, from human Glutaredoxin 1 expressed in E.coli.\n\nMolecular Weight:\n~11.8kD\n\nSpecific Activity:\n130U/mg (One unit will cause the oxidation of 1umole of NADPH per min)\n\nStorage and Stability:\nAliquot to avoid repeated freezing and thawing and store at -70 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

G5011-01

Size

100ug

Form

Supplied as a liquid in 20mM HEPES, pH7.0, 10% glycerol.

Purity

~95% (SDS-PAGE)

References

1. Holmgren, A. (1990) p. 146-154, CRC Press Inc., Boca Raton, FL 2. Holmgren, A. (1989) J. Biol. Chem. 264, 13963-13966. 3. Jung, C. H. and Thomas, J. A. (1996) Arch. Biochem. Biophys. 335, 61-72. 4. Alexios, V. et al. (1997) J. Biol. Chem. 272, 11236-11243.

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