Specific activity is > 20unit/mg, and is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.
Preparation
Liquid purified protein
Recommended Dilution
SDS-PAGE, Enzyme Activity
Protein Description
Recombinant GST was expressed in E.coli and purified by conventional chromatography techniques.
Storage
Can be stored at +2°C to +8°C for 1 week. For long term storage, aliquot and store at -20°C to -80C. Avoid repeated freezing and thawing cycles.
Glutathione S-transferase (GST) represents a major group of detoxification enzymes. This enzyme acts by catalyzing the reaction of glutathione with an acceptor molecule to form an S-substituted glutathione (S=sulfur). The reactions utilizing glutathione contribute the transformation of a wide range of compounds, including carcinogens, therapeutic drugs, and products of oxidative stress. As well as its enzymatic activities, GST may also bind toxins and function as transport protein. Because of this, an early term for GSTs was ligandin. Glutathione S-transferase was originally separated from Schistosoma japonicum but currently isolated from recombinant E. coli source. Recombinant GST was expressed in E. coli and purified by conventional chromatography techniques.
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