L-Glutathione reduced (Glutathione) is a naturally occurring tripeptide found in cells as an endogenous antioxidant that scavenges oxygen free radicals. L-Glutathione reduced is a cofactor for certain enzymes and is involved in the rearrangement of protein disulfide bonds and the reduction of peroxides.

Glutathione oxidized (L(-) -glutathione) is the oxidized form of Glutathione, which is a major antioxidant and antidote in cells. Glutathione oxidized can be used to study sickle cells and red blood cells.

LCS3 is a reversible and non-competitive synergistic inhibitor of glutathione disulfide reductase (GSR) and thioredoxin reductase 1 (TXNRD1) with IC50s of 3.3 μM and 3.8 μM, respectively. LCS3 has antitumour activity, induces apoptosis and can be used in the study of lung adenocarcinoma (LUAD).

Nitrofurazone (Nitrofural; Furacilin) is an orally active nitroaromatic broad-spectrum antibiotic with activity against both Gram-positive and Gram-negative bacteria. It is commonly used for establishing breast cancer models.

Glutathione Reductase, Wheat germ (EC 1.6.4.2), is a crucial flavoprotein in the antioxidant defense system. In this process, reduced glutathione (GSH) detoxifies hydrogen peroxide via glutathione peroxidase, becoming oxidized to form oxidized glutathione (GSSG). Glutathione Reductase (GR) then reduces GSSG back to GSH using NADPH, which is converted to NADP+. The regenerated GSH is available for further hydrogen peroxide detoxification. Glutathione Reductase utilizes FAD as a cofactor.

Dantrolene-13C3 is the 13C3-labeled form of Dantrolene. Dantrolene (T8452) (F368) serves as a muscle relaxant and non-competitively inhibits human erythrocyte glutathione reductase (glutathione reductase), exhibiting Ki and IC50 values of 111.6 μM and 52.3 μM, respectively. Additionally, Dantrolene (T8452) acts as a ryanodine receptor antagonist and a stabilizer of Ca2+ signals. It is utilized in the treatment of muscle spasms and malignant hyperthermia.

Glutathione Reductase, Wheat germ (EC 1.6.4.2), is an essential flavoprotein in the antioxidant defense system. The reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide, during which it is oxidized to form oxidized glutathione (GSSG). The GSSG is then reduced back to GSH by glutathione reductase (GR) using NADPH, which is converted to NADP+ in the process. The regenerated GSH can continue detoxifying hydrogen peroxide. Glutathione Reductase utilizes FAD as a cofactor.