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Key Documents

CS1020

Sigma-Aldrich

Glutathione Assay Kit, Fluorimetric

sufficient for 200 multiwell tests

Synonym(s):

GSH Quantification Kit

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About This Item

EC Number:
UNSPSC Code:
12161503
NACRES:
NA.84

usage

sufficient for 200 multiwell tests

Quality Level

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... GSTA4(2941)

Application

Glutathione Assay Kit, Fluorimetric has been used in intracellular thiol assays and in the measurement of hepatic glutathione in rats.
The Glutathione Assay Kit, Fluorimetric includes all the reagents required for fast and easy measurement of reduced glutathione in cell or tissue extracts or directly in growing cells. Staurosporine is supplied with the kit to enable induction of apoptosis in cells. Since the amount of reduced glutathione in staurosporine-induced cells is significantly lower than in non-induced cells, this can serve as a control system.

Biochem/physiol Actions

Glutathione (GSH) acts as a cofactor for several antioxidant enzymes. It helps in the regeneration of vitamins C and E. It regulates cellular proliferation and apoptosis. GSH is important for mitochondrial functioning and the maintenance of mitochondrial DNA (mtDNA). Mutations in this gene is associated with Alzheimer′s, Parkinson′s and Huntington′s diseases.
Reduced glutathione (GSH), a tripeptide (γ-glutamyl-cysteinylglycine), is the major free thiol in most living cells and is involved in many biological processes such as detoxification of xenobiotics, removal of hydroperoxides, and maintenance of the oxidation state of protein sulfhydryls. It is the key antioxidant in animal tissues. Glutathione is present inside cells primarily in the reduced form (90-95% of the total glutathione). The remainder is present in the oxidized form (glutathione disulfide, GSSG). Intracellular GSH status appears to be a sensitive indicator of the overall health of a cell and its ability to resist toxic challenge. High levels of GSH in the cell may indicate pathological changes.

Analysis Note

The kit assay utilizes a thiol probe (monochlorobimane), which can freely pass through the plasma membrane. The free, unbound probe shows very little fluorescence, but when bound to reduced glutathione in a reaction that is catalyzed by glutathione S-transferase (GST), it forms a strongly fluorescent adduct.

Kit Components Only

Product No.
Description

  • Assay Buffer 50 mL

  • Substrate Solution 1 mL

  • Lysis Buffer 10x 1.5 mL

  • Glutathione S-Transferase 1 mL

  • Staurosporine Ready Made 100 μL

  • Glutathione, reduced 300 mg

related product

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Sadeghi B.
Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy, 118, 787-792 (2014)
Elzbieta Zieminska et al.
Neurochemical research, 42(3), 777-787 (2016-10-09)
Using primary cultures of rat cerebellar granule cells (CGC) we examined the role of calcium transients induced by tetrabromobisphenol A (TBBPA) in triggering oxidative stress and cytotoxicity. CGC were exposed for 30 min to 10 or 25 µM TBBPA. Changes in intracellular
Mehdi Hichor et al.
Scientific reports, 8(1), 2524-2524 (2018-02-08)
Reactive oxygen species (ROS) modify proteins and lipids leading to deleterious outcomes. Thus, maintaining their homeostatic levels is vital. This study highlights the endogenous role of LXRs (LXRα and β) in the regulation of oxidative stress in peripheral nerves. We
Glutathione: Physiological and clinical relevance
Pizzorno JE and Katzinger JJ
Journal of restorative medicine, 1(1), 24-37 (2012)
Shayne Squires et al.
The open biochemistry journal, 7, 54-65 (2013-08-07)
We investigated whether a cell-penetrating peptide linked via a disulfide bond to a fluorophore-labeled cargo peptide can be used to interrogate changes in cellular redox state. A fluorescence resonance energy transfer (FRET) pair was constructed so that the cargo peptide

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