Thioredoxin Reductase, Yeast, Recombinant, E. coli

Toxicity: Standard Handling (A)

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.

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.

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.

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