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Key Documents

G4251

Sigma-Aldrich

L-Glutathione reduced

≥98.0%

Sinonimo/i:

Glutathione-SH, γ-L-Glutamyl-L-cysteinyl-glycine, GSH

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About This Item

Formula condensata:
H2NCH(CO2H)CH2CH2CONHCH(CH2SH)CONHCH2CO2H
Numero CAS:
Peso molecolare:
307.32
Beilstein:
1729812
Numero CE:
Numero MDL:
Codice UNSPSC:
12352209
ID PubChem:
NACRES:
NA.26

product name

L-Glutathione reduced, ≥98.0%

Livello qualitativo

Saggio

≥98.0%

Forma fisica

powder

Colore

white

Punto di fusione

192-195 °C (dec.) (lit.)

Solubilità

water: 50 mg/mL, clear, colorless

applicazioni

detection

Gruppo funzionale

amine
carboxylic acid
thiol

Temperatura di conservazione

2-8°C

Stringa SMILE

N[C@@H](CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O)C(O)=O

InChI

1S/C10H17N3O6S/c11-5(10(18)19)1-2-7(14)13-6(4-20)9(17)12-3-8(15)16/h5-6,20H,1-4,11H2,(H,12,17)(H,13,14)(H,15,16)(H,18,19)/t5-,6-/m0/s1
RWSXRVCMGQZWBV-WDSKDSINSA-N

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Amino Acid Sequence

γ-Glu-Cys-Gly

Descrizione generale

Glutathione (GSH) is a ubiquitous molecule found in many cells and tissues. The three amino acids present in GSH are glycine, cysteine, and glutamic acid.

Applicazioni

L-Glutathione (GSH) reduced has been used in the elution buffer to elute GST (glutathione S-transferase)-fused proteins using glutathione-agarose beads. It has been used to prepare a standard curve for GSH analyses.
May be used at 5-10 mM to elute glutathione S-transferase (GST) from glutathione agarose.

Azioni biochim/fisiol

Glutathione (GSH) forms conjugates with various metabolites and xenobiotics. It acts as an important co-factor for various enzymes. GSH is involved in many metabolic and signaling pathways. Glutathione functions as a thiol buffer for cellular proteins like thioredoxins and metallothioneins. GSH is also involved in the regeneration of antioxidants like tocopherols and ascorbate.
Endogenous antioxidant that plays a major role in reducing reactive oxygen species formed during cellular metabolism and the respiratory burst. Glutathione-S-transferase catalyzes the formation of glutathione thioethers with xenobiotics, leukotrienes, and other molecules that have an electrophilic center. Glutathione also forms disulfide bonds with cysteine residues in proteins. Via these mechanisms, it can have the paradoxical effect of reducing the efficacy of anti-cancer agents.

Altre note

For additional information on our range of Biochemicals, please complete this form.

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Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 2

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)


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Hee Woong Yang et al.
FEBS letters, 593(15), 2060-2068 (2019-06-11)
Ribosomal protein S3 (rpS3) has endonuclease activity for DNA repair. In particular, rpS3 cleaves the phosphodiester bonds of damaged DNA. In this study, we show that the repair domain of rpS3 spans amino acids 144-189. We fused rpS3 with the
Nitric oxide as an independent regulatory factor in regenerating rat liver.
Tuncyurek P, et al.
Acta Chirurgica Belgica, 106, 581-581 (2006)
Cu 2 O/NiO x/graphene oxide modified glassy carbon electrode for the enhanced electrochemical oxidation of reduced glutathione and nonenzyme glucose sensor.
Yuan B et al.
Electrochimica Acta, 104, 78-78 (2013)
Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent-free purification of caveolae microdomains.
Song KS, et al.
The Journal of Biological Chemistry, 271, 9690-9690 (1996)
Surface Plasmon Resonance (SPR) Analysis of Binding Interactions of Inner-Ear Proteins.
Drescher DG, et al.
Methods in Molecular Biology, 1427, 165-165 (2016)

Articoli

Oxidative stress is mediated, in part, by reactive oxygen species produced by multiple cellular processes and controlled by cellular antioxidant mechanisms such as enzymatic scavengers or antioxidant modulators. Free radicals, such as reactive oxygen species, cause cellular damage via cellular.

Antioxidants protect biological systems from oxidative damage produced by oxygen-containing free radicals and from redoxactive transition metal ions such as iron, copper, and cadmium.

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