Glutathione S-Transferase from E. coli

Glutathione S-transferase (GST) catalyzes the addition of the glutathione thiol group to a suitable electrophilic species. Enzymatic activities are based on the conjugation of reduced glutathione in the presence of a second substrate.

Glutathione S-Transferase (GST) from E. coli has been used in the standard curve preparation for the quantification of GST-V5H6 produced by enzyme-linked immunosorbent assay (ELISA).

Suitable for use in ELISA and Western blot applications.

Glutathione S-transferases (GST) catalyzes the conjugation of reduced glutathione with several substrates, which leads to detoxification. It also serves as transport proteins.

Glutathione S-transferase (GST) catalyzes the addition of the glutathione thiol group to a suitable electrophilic species. Enzymatic activities are based on the conjugation of reduced glutathione in the presence of a
second substrate.

In ELISA, 0.5 μg of recombinant glutathione S-transferase is the minimum detectable level of enzyme with an anti-glutatione S-transferase, alkaline phosphatase conjugate.

In immunoblot, 50 ng of recombinant GST is the minimum detectable level of enzyme with an anti-glutathione S-transferase, alkaline phosphatase conjugate.

GST is supplied as a solution in phosphate buffered saline containing 0.02% sodium azide. Every lot of material supplied will have 5 mg total enzyme, at a concentration greater than 0.1 mg/ml, typically 1.0 mg/ml.

One unit will conjugate 1.0 micromole of 1-chloro-2,4-dinitrobenzene with reduced glutathione per minute at pH 6.5 at 25 deg C.

Due to the sodium azide content, consult the SDS for information regarding hazards and safe handling practices.