Active • Host: E. coli • AA: 598 residues
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Thioredoxin Glutathione Reductase (Schistosoma mansoni, recombinant)

Item No. 39632

Technical Information
Synonyms
  • TGR
Purity
≥95% estimated by SDS-PAGE
Source
Active recombinant S. mansoni TGR expressed in E. coli
Amino Acids
598 residues
250 µg protein in TE buffer with 50% glycerol
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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    Product Description

    Thioredoxin glutathione reductase (TGR) is a selenocysteine-containing oxidoreductase flavoenzyme that protects Schistosoma, the genus of blood flukes that causes schistosomiasis, and other helminth parasites from host-induced oxidative damage.1,2 It is a homodimer that contains an N-terminal glutathione reductase domain, an FAD- and NADPH- binding site, and a thioredoxin domain near the C-terminus, and it can reduce both DTNB and oxidized glutathione (GSSH).2 TGR catalyzes NADPH- and FAD-dependent reduction of oxidized thioredoxin (Trx), glutathione (GSH), and glutaredoxin (Grx), which mitigate the effects of reactive oxygen and nitrogen species released by host neutrophils and macrophages that can damage intracellular proteins and lipids.3 Cayman's TGR (Schistosoma mansoni, recombinant) protein can be used for enzyme activity assays.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Alger, H.M., and Williams, D.L. The disulfide redox system of Schistosoma mansoni and the importance of a multifunctional enzyme, thioredoxin glutathione reductase. Mol. Biochem. Parasitol. 121(1), 129-139 (2002).

    2. Angelucci, F., Miele, A.E., Boumis, G., et alGlutathione reductase and thioredoxin reductase at the crossroad: The structure of Schistosoma mansoni thioredoxin glutathione reductase. Proteins 72(3), 936-945 (2008).

    3. Williams, D.L., Bonilla, M., Gladyshev, V.N., et alThioredoxin glutathione reductase-dependent redox networks in platyhelminth parasites. Antioxid. Redox Signal. 19(7), 735-745 (2013).