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Glutathione Reductase, Recombinant, Human (Glutathione Reductase, Mitochondrial, GR, GRase, GSR, GLUR, GRD1)

Cat no: G8127-19P

Glutathione Reductase, Recombinant, Human (Glutathione Reductase, Mitochondrial, GR, GRase, GSR, GLUR, GRD1)

Glutathione reductase (GR) is a member of pyridine nucleotide-disulfide oxidoreductases, which includes the closely related enzymes thioredoxin reductase, lipoamide dehydrogenase, trypanothione reductase and mercuric ion reductase. GR is a cytoplasmic flavoenzyme widely distributed in aerobic organisms. The dimeric protein is composed of two identical subunits, each containing 1 FAD and 1 redox-active disulfide/dithiol as components of the catalytic apparatus. It plays a role in maintaining glutathione (GSH) in its reduced form by catalyzing the reduction of glutathione disulfide (GSSG) (1): GSSG + NADPH + H+ 2GSH + NADP+ In most eukaryotic cells, GR maintains the ratio of [GSH]/[GSSG] elevated, and participates in several vital functions such as the detoxification of reactive oxygen species as well as protein and DNA biosynthesis (2).\n\nSource:\nRecombinant corresponding to aa44-522 with additional 3aa-GSH at N-term, from human Glutathione Reductase, expressed in E.coli.\n\nMolecular Weight:\n~51.7kD\n\nSpecific Activity:\n19.4U/mg (One unit will reduce 1umole of oxidized glutathione per min at pH 7.5 at 25 degrees C)\n\nStorage and Stability:\nLyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

G8127-19P

Size

500ug

Form

Supplied as a lyophilized powder from 20mM HEPES, pH 7.4. Reconstitute with sterile dH2O PBS.

Purity

~95% (SDS-PAGE)

References

1. Carlberg, I. and Mannervik, B. (1985) J. Biol. Chem. 261: 1629-1635. 2. Picaud, T. and Desbois, A. (2002) J. Biol. Chem. 277: 31715-31721.

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