Glutathione Detection Kit
The Glutathione Detection Kit is For Research Use Only
Size: 1×96 wells
Sensitivity: 45 nM in the Free GSH and 48 nM in the Total GSH
Dynamic Range: 0.195 – 25 uM
Incubation Time: 30 minutes
Sample Type: Cell lysates, EDTA Plasma, Erythrocytes, Heparin Plasma, Serum, Tissue, Urine, Whole Blood
Sample Size: 50 μL
Product manufactured in Canada by StressMarq.
Glutathione (L-γ-glutamyl-L-cysteinylglycine; GSH) is the highest concentration non-protein thiol in mammalian cells and is present in concentrations of 0.5 – 10 mM (1). GSH plays a key role in many biological processes, including the synthesis of proteins and DNA, the transport of amino acids, and the protection of cells against oxidation. Harmful hydrogen peroxide cellular levels are minimized by the enzyme glutathione peroxidase (GP) using GSH as a reductant (2). The oxidized GSH dimer, GSSG, is formed from GSH and peroxide by the GP reaction (see below). An important role of GSSG in the NFγB activating signal cascade is suggested by the facts that the potent NFγB inducer, tetradecanoyl phorbol acetate, increases intracellular GSSG levels and GSSG/GSH ratios (3). Glutathione S-transferases (GST) are an important group of enzymes that catalyze the nucleophilic addition of GSH to electrophiles. They are encoded by 5 gene families; 4 encode cytosolic GST and one encodes the microsomal form of GST. They have been implicated in a number of diseases. In asthma arachidonic acid is converted to unstable leukotriene A4 (LTA4). LTA4 is either hydrated to form LTB4 or it is conjugated to GSH by a GST, leukotriene C4 synthase, to form leukotriene C4. LTC4 and its derivative LTD4 are important molecules in bronchial asthma. Leukotriene C4 synthase is therefore an important therapeutic target. It has also been shown that increased expression of GSTs can lead to drug resistance. Three glutathione adducts of the drug melphalan, used to treat ovarian cancer and multiple myeloma, have been isolated from reactions involving human microsomal GSTs.