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 human GST, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.
Source:Recombinant corresponding to human GST, his-tagged, expressed in E. coli.
Enzyme Activity: Specific activity is > 10 units/mg, and is defined as the amount of enzyme that conjugates 1.0 umole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25°C.
Storage and Stability:May be stored at 4°C for short-term only. For long-term storage, aliquot and store at -20°C. Aliquots are stable for at least 6 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
仕様
Size：100ug
Source Antigen：Recombinant, E.coli
Grade：Affinity Purified
Purity：~95% (SDS-PAGE) Purified by immunoaffinity chromatography.
Form：Supplied as a liquid in PBS, pH7.4, 10% glycerol.
