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G5663

Sigma-Aldrich

Glutathione S-Transferase from E. coli

recombinant, expressed in E. coli, buffered aqueous solution

Synonyme(s) :

Glutathione S-alkenetransferase, Glutathione S-alkyltransferase, Glutathione S-aralkyltransferase, Glutathione S-aryltransferase, Glutathione S-epoxidetransferase, RX: Glutathione R-transferase

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About This Item

Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.53

Produit recombinant

expressed in E. coli

Qualité

for molecular biology

Forme

buffered aqueous solution

Poids mol.

26 kDa

Concentration

>0.1 mg/mL
>1 unit/mL

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Informations sur le gène

human ... GSTM1(2944)

Description générale

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.

Spécificité

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.

Application

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.

Actions biochimiques/physiologiques

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

Avertissement

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

Définition de l'unité

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.

Forme physique

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.

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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