GST T2-2 Recombinant Protein

Recombinant 6x His-tagged protein expressed in E Coli.

>= 95% as assessed by inspection on a Coomassie Blue-stained SDS-PAGE gel.

1.91 mg/mL total protein using the Bradford protein assay with BSA as a standard. (lot specific)

Specific Activity: 12.6 Units/mg as assayed by the spectrophotometric determination of NADPH oxidation coupled to the glutathione peroxidase activity of GST T2-2 on cumene hydroperoxide (1.5 mM) in the presence of reduced glutathione (1 mM) in 100 mM NaPO4 (pH 7.0) at room temperature.

At -20 degree C; AVOID MULTIPLE FREEZE-THAW CYCLES.

~25 kDa

50 mM Tris-HCl (pH 7.5), 50 mM NaCl, 1 mM DTT, 1 mM EDTA and 50% glycerol.

This purified product exhibits moderate enzymatic activity for Cumene hydroperoxide, the substrate that is most commonly used to assess the glutathione peroxidase activity of soluble GSTs. However, as is suspected for GST activity analysis using synthetic and natural substrates, low concentrations (high dilutions) of the enzyme may result in lower activity values. In contrast, initial velocities are much higher for more concentrated levels of enzyme but the rate decreases rapidly. Therefore, activity towards GST substrates and these considerations provide guidance when assaying this product under low concentrations or when using substrates other than Cumene hydroperoxide.