The TGR selenoprotein of Schistosoma mansoni is the only major reductive cytosolic flavoprotein of this parasite, taking over the combined role of TrxR1 and glutathione reductase, thereby exerting a wide range of functions in redox control and antioxidant systems and being a promising drug target for treatment of schistosomiasis.
We provide the main the Schistosoma mansoni TGR enzyme with more than 90% Sec contents and more than 95% purity in aliquots at amounts from 5 to 50 units.

• Genuine Sec-containing selenoproteins
• No animals used as protein sources (grown in bacteria)
• More than 90% Sec contents
• More than 95% purity

Recombinant Shistosoma Mansoni Thioredoxin Glutathione Reductase (Non-tagged, 598 residues)

5 (10, 20, 50) Units, ca 0.25 (0.5, 1, 2.5) mg protein stored in TE buffer with 50% glycerol. Concentration 1 mg/ml.

1 U of enzyme reduces 1 μmol DTNB per min in 0.5 ml standard DTNB assay containing 2.5 mM DTNB and 0.3 mM NADPH in TE buffer (50 mM Tris-HCl, 2 mM EDTA, pH 7.5)

References: Cheng Q, Arnér ES. (2017) Selenocysteine Insertion at a Predefined UAG Codon in a Release Factor 1 (RF1)-depleted Escherichia coli Host Strain Bypasses Species Barriers in Recombinant Selenoprotein Translation. J Biol Chem. 292:5476-5487.
Arnér ES, Holmgren A. (2001) Measurement of thioredoxin and thioredoxin reductase. Curr Protoc Toxicol. Chapter 7:Unit 7.4.