glutathione disulfide

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.

L-Cysteine-glutathione disulfide is a potential biomarker for curing tuberculosis, present in mammalian cells with hepatoprotective effects, useful in acetaminophen-induced liver toxicity research.

Glutathione-CoA, disulfide (Coenzyme A-glutathione mixed disulfide) is a derivative of coenzyme A.

Glutathione Oxidized-13C4,15N2 (Standard) is a reference standard of Glutathione Oxidized-13C4,15N2 intended for quantitative analysis, quality control, and related biochemical research applications. Glutathione oxidized-13C4,15N2 is the 13C and 15N labeled form of Glutathione oxidized. This compound is the product of glutathione oxidation, which occurs during the detoxification of reactive oxygen species. It is utilized in the research of sickle cells and erythrocytes (red blood cells).

Glutathione arsenoxide hydrochloride (Glutathione arsenoxide hydrochloride(1271726-51-2 Free base)) is a potentially active anti-cancer molecule and inhibitor of tumour metabolism. glutathione arsenoxide hydrochloride targets the mitochondrial inner membrane adenine nucleotidyl transferase (ANT), which inhibits cell proliferation and promotes apoptosis. Glutathione arsenoxide hydrochloride can be used to recognize cell surface proteins such as protein disulfide isomerases.

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.

TDK-HCPT is a small molecule conjugate that links glutathione-sensitive thiamine disulfide with the chemotherapeutic agent 10-hydroxycamptothecin through a thioacetal bond. It targets tumor cells and prolongs the retention of the chemotherapeutic drug within these cells. TDK-HCPT inhibits tumor growth, induces apoptosis (apoptosis) in tumor cells, and exhibits antitumor activity.

TrxR-IN-8 (Compound 6f) is a selective inhibitor of TrxR with an IC50 of 10.2 μM. It induces apoptosis through oxidative stress by stimulating the production of reactive oxygen species, reducing intracellular thiols, and lowering the glutathione/glutathione disulfide ratio. TrxR-IN-8 exhibits significant cytotoxicity against non-small cell lung cancer (NSCLC) cells.

Glutathione arsenoxide (GSAO) TFA is a potential anticancer agent and tumor metabolism inhibitor. It specifically targets the adenine nucleotide translocase (ANT) on the mitochondrial inner membrane. This compound induces cell proliferation arrest and cell death. Additionally, Glutathione arsenoxide TFA can be utilized to identify cell surface proteins, including protein disulfide isomerase.

Ophthalmic acid is a ubiquitous metabolite and glutathione modulator with a Ki value of 0.95 mM for glyoxalase I. Ophthalmic acid competitively inhibits glyoxalase I, glutathione S-transferase, glutaredoxin, glutamate-cysteine ligase, protein disulfide reductase (glutathione), and non-selective cation channels. Ophthalmic acid is applicable to diabetes-related investigations and is particularly valuable for studies involving oxidative stress, glutathione metabolism, redox regulation, and metabolic dysfunction.

Glutathione can occur in reduced (GSH), oxidized (GSSG), or in mixed disulfide forms and is ubiquitous in multiple biological systems serving as the major thiol-disulfide redox buffer of the cell. GSSG is the oxidized form of GSH . It can be reduced back to GSH through the NADPH-dependent enzyme glutathione reductase. GSSG functions as a hydrogen acceptor in the enzymatic determination of NADP+ and NADPH and can be a proximal donor in S-glutathionylation post translational modifications. The ratio of reduced glutathione to oxidized glutathione within cells is often used as an indicator of oxidative stress, with higher concentrations of GSSG predicting increased oxidative stress.

(E)-Ajoene is a disulfide that has been found inA. sativumand has diverse biological activities.1,2,3,4It is active against Gram-positive and Gram-negative bacteria (MICs = 10-250 and 150->500 μg/ml, respectively) and fungi (MICs = 15-50 μg/ml).1(E)-Ajoene inhibits proliferation of a variety of cancer cells, including MDA-MB-231 breast, HeLa cervical, and WHCO1 esophageal cancer cells (IC50s = 18.6, 61, and 39.2 μM, respectively).2It also inhibits human glutathione reductase andT. cruzitrypanothione reductase when used at a concentration of 200 μM.3(E)-Ajoene (25 mg/kg) is neuroprotective in a gerbil model of ischemia-reperfusion injury, reducing reactive astrocytosis and microgliosis in the hippocampal CA1 region.4 1.Yoshida, H., Iwata, N., Katsuzaki, H., et al.Antimicrobial activity of a compound isolated from an oil-macerated garlic extractBiosci. Biotechnol. Biochem.62(5)1014-1017(1998) 2.Kaschula, C.H., Hunter, R., Hassan, H.T., et al.Anti-proliferation activity of synthetic ajoene analogues on cancer cell-linesAnticancer Agents Med. Chem.11(3)260-266(2011) 3.Gallwitz, H., Bonse, S., Martinez-Cruz, A., et al.Ajoene is an inhibitor and subversive substrate of human glutathione reductase and Trypanosoma cruzi trypanothione reductase: Crystallographic, kinetic, and spectroscopic studiesJ. Med. Chem.42(3)364-372(1999) 4.Yoo, D.Y., Kim, W., Nam, S.M., et al.Neuroprotective effects of Z-ajoene, an organosulfur compound derived from oil-macerated garlic, in the gerbil hippocampal CA1 region after transient forebrain ischemiaFood Chem. Toxicol.721-7(2014)

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).

Glutathione Peroxidase (GSH-Px; EC 1.11.1.9), a member of the peroxidase family, catalyzes the oxidation of reduced glutathione (GSH) to oxidized glutathione (GSSG) by forming a disulfide bridge, while concurrently reducing hydrogen peroxide or lipid peroxides to water, serving as a potent antioxidant and protecting against oxidative stress [1].

L-Glutathione reduced (Standard) is a reference standard for research and analysis in studies involving L-Glutathione reduced. 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.

Thioredoxin reductase peptide, corresponding to residues 53-67 in thioredoxin reductase (TrxR), is used in thioredoxin reductase research. Mammalian thioredoxin reductase (TR) catalyzes the reduction of the redox-active disulfide bond of thioredoxin (Trx) and is structurally and mechanistically similar to glutathione reductase, except for a C-terminal 16-amino acid extension containing a rare vicinal selenylsulfide bond.

Thioredoxin reductase peptide acetate corresponds to residues 53–67 in thioredoxin reductase (TrxR), used in thioredoxin reductase research.Mammalian thioredoxin reductase (TR) catalyzes the reduction of the redox-active disulfide bond of thioredoxin (Trx