||The protein encoded by this gene acts as a homodimer and is involved in many redox reactions. The encoded protein is active in the reversible S-nitrosylation of cysteines in certain proteins, which is part of the response to intracellular nitric oxide. This protein is found in the cytoplasm. Two transcript variants encoding different isoforms have been found for this gene.
||Lyophilized from 34 µl 50 mM tris-Cl, pH 7.5, 1 mM EDTA.
||Activity can be measured with the thioredoxin-dependent reduction of insulin using recombinant rat thioredoxin reductase. The test mixture should contain 160 µM insulin and 0.2 mM NADPH in 0.1 M potassium phosphate, pH 7.0, containing 2 mM EDTA. In the presence of 5 µM human thioredoxin, 7 nM mammalian thioredoxin reductase will give an absorbance decrease of 0.10/min at 340 nm.
||Make sure to reconstitute all of the lyophilized protein in the ampoule. After adding buffer, close the screw-cap again, shake vigorously, then centrifuge shortly, in order to recover liquid from tube cap and walls.
||Keep at 4 centigrade or alternatively reconstituted protein in aliquots at -20 centigrade.
||Reconstitute with 100 µl H2O. This gives a solution of 210 µM thioredoxin. The protein is oxidized ( two disulfides) and can be reactivated by addition of a 5-fold molar excess of DTT. Alternately incubate with NADPH and TrxR.