Active • Host: E. coli • AA: 488 residues
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Thioredoxin Reductase 2 (human, recombinant)

Item No. 39625

Product Insert (PDF)
Technical Information
Synonyms
  • NADPH-dependent Thioredoxin Reductase 2
  • TrxR2
  • Txnrd2
Purity
≥95% estimated by SDS-PAGE
Source
Active recombinant human TrxR2 expressed in E. coli
Amino Acids
488 residues
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 reductase 2 (TrxR2) is an oxidoreductase encoded by the TXNRD2 gene in humans and a member of the antioxidant thioredoxin system.1 It exists as a homodimer and contains a dimer interface 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 TrxR2.1,2 TrxR2 is ubiquitously expressed and localizes primarily to the mitochondria.3 It catalyzes the NADPH-dependent reduction of oxidized thioredoxin 2 (Trx2), restoring the disulfide reductase function of Trx2, which reduces peroxiredoxin-3 (Prx3) dimers.4,5 TrxR2 has roles in the maintenance of mitochondrial integrity and redox homeostasis in the aging heart and in the regulation of chondrocyte viability, proliferation, and differentiation.2 Genome-wide deletion of Txnrd2 is embryonic lethal in mice.6 TXNRD2 expression and TrxR2 protein levels are increased in bone biopsies from patients with osteosarcoma that later progress to metastatic disease.7 SNPs in TXNRD2 are associated with serum markers of selenium status in patients with advanced- or high-stage, but not localized low-grade, prostate cancer.8 Cayman’s Thioredoxin Reductase 2 (human, 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. Mustacich, D., and Powis, G. Thioredoxin reductase. Biochem. J. 346(Pt. 1), 1-8 (2000).

    2. Scalcon, V., Bindoli, A., and Rigobello, M.P. Significance of the mitochondrial thioredoxin reductase in cancer cells: An update on role, targets and inhibitors. Free Radic. Biol. Med. 127, 62-79 (2018).

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

    4. Holmgren, A., and Lu, J. Thioredoxin and thioredoxin reductase: Current research with special reference to human disease. Biochem. Biophys. Res. Commun. 396(1), 120-124 (2010).

    5. Watanabe, R., Nakamura, H., Masutani, H., et alAnti-oxidative, anti-cancer and anti-inflammatory actions by thioredoxin 1 and thioredoxin-binding protein-2. Pharmacol. Ther. 127(3), 261-270 (2010).

    6. Conrad, M., Jakupoglu, C., Moreno, S.G., et alEssential role for mitochondrial thioredoxin reductase in hematopoiesis, heart development, and heart function. Mol. Cell. Biol. 24(21), 9414-9423 (2004).

    7. Topkas, E., Cai, N., Cumming, A., et alAuranofin is a potent suppressor of osteosarcoma metastasis. Oncotarget 7(1), 831-844 (2016).

    8. Méplan, C., Rohrmann, S., Steinbrecher, A., et alPolymorphisms in thioredoxin reductase and selenoprotein K genes and selenium status modulate risk of prostate cancer. PLoS One 7(11), e48709 (2012).