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Item No. 39632

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Explore how neutrophils shape the immune response in health and disease. This poster highlights neutrophil pathogen defense mechanisms, including phagocytosis, degranulation, and NETosis, as well as neutrophil roles in inflammation and NET-associated pathologies.
DOWNLOAD NOWThioredoxin 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.
1. 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. Glutathione reductase and thioredoxin reductase at the crossroad: The structure of Schistosoma mansoni thioredoxin glutathione reductase. Proteins 72(3), 936-945 (2008).
3. Thioredoxin glutathione reductase-