Thioredoxin Reductase 1 (C. elegans, recombinant)

Thioredoxin reductase 1 (TrxR1) is a selenocysteine-containing oxidoreductase and the only selenoprotein in C. elegans.¹ It contains a dimerization domain, FAD- and NADPH-binding domains, an N-terminal redox catalytic site, and a C-terminal selenocysteine residue, which is essential for the catalytic activity of TrxR1. TrxR1 is expressed in the hypodermis, pharynx, vulva, intestine, and nervous system and localizes to the cytoplasm in C. elegans.^1,2 Knockout of trxr1 sensitizes C. elegans to oxidative stress in a context-dependent manner and does not affect C. elegans lifespan, brood size, or molting.^3,1 However, double knockout of trxr1 and the gene encoding glutathione reductase (gsr1) induces arrest at the molting stage, an effect that can be rescued by exogenous glutathione (GSH).¹ Increased serum TrxR1 activity is associated with reduced progression-free survival in patients with non-small cell lung cancer (NSCLC).⁴ Cayman's Thioredoxin Reductase 1 (C. elegans, recombinant) protein can be used for enzyme activity assays.

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1. Stenvall, J., Fierro-González, J.C., Swoboda, P., et al. Selenoprotein TRXR-1 and GSR-1 are essential for removal of old cuticle during molting in Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA 108(3), 1064-1069 (2011).

2. Li, W., Bandyopadhyay, J., Hwaang, H.S., et al. Two thioredoxin reductases, trxr-1 and trxr-2, have differential physiological roles in Caenorhabditis elegans. Mol. Cells 34(2), 209-218 (2012).

3. Rohn, I., Raschke, S., Aschner, M., et al. Treatment of Caenorhabditis elegans with small selenium species enhances antioxidant defense systems. Mol. Nutr. Food Res. 63(9), e1801304 (2019).

4. Chen, G., Chen, Q., Zeng, F., et al. The serum activity of thioredoxin reductases 1 (TrxR1) is correlated with the poor prognosis in EGFR wild-type and ALK negative non-small cell lung cancer. Oncotarget 8(70), 115270-115279 (2017).