ferredoxin glutathione reductase Structure of homodimer where one binds to reduced nicotinamide adenine dinucleotide phosphate (NADPH) and flavin adenine dinucleotide (FAD) the second one is an interface dimerization domain Sigma-Aldrich Glutathione Reductase human, CAS
Sigma Aldrich Glutathione Reductase human, CAS 9001 48 3, buffered aqueous solution, 10 units mg protein, recombinant, expressed in E. coli 500 ug Glutaredoxin catalysis requires two distinct glutathione interaction sites Nature Communications A distinct class of ferredoxin:NADP+ oxidoreductase enzymes driving thermophilic ethanol production Journal of Biological Chemistry Frontiers Progress in the study of the mechanism of ferroptosis in coronary heart disease and clinical intervention strategies Non covalent inhibitors of thioredoxin glutathione reductase with schistosomicidal activity in vivo Nature Communications
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