Thioredoxin Reductase, Yeast, Recombinant, E. coli

Recombinant, yeast thioredoxin reductase expressed in E. coli. Yeast thioredoxin reductase is a flavoprotein that has no selenocysteine (SeCys). It catalyzes the NADPH-dependent reduction of thioredoxin as well as other endogenous and exogenous proteins. Plays an important role in many aspects of cell function, including protection against oxidative stress/injury, cell growth and transformation, and the recycling of ascorbate from its oxidized form.

Toxicity: Standard Handling (A)

One unit is defined as the amount of enzyme that will cause an absorbance change of 1 at 412 nm using 200 µM NADPH and 5 mM DTNB, per min at 25°C, pH 7.0.

Lyophilized from 150 mM NaCl, 20 mM phosphate buffer, pH 7.4.

Following reconstitution, aliquot and freeze (-70°C). Stock solutions are stable for 1 month at 4°C or 3 months at -70°C.

Mustacich, D. and Powis, G. 2000. Biochem. J.346, 1.
Wang, P.F., et al. 1998. Biochemistry37, 16378.
Holmgren, A., 1979. J. Biol. Chem. 254, 9627.

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