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G5663

Sigma-Aldrich

Glutathione S-Transferase from E. coli

recombinant, expressed in E. coli, buffered aqueous solution

Synonym(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

MDL number:
UNSPSC Code:
12352204
NACRES:
NA.53

recombinant

expressed in E. coli

grade

for molecular biology

form

buffered aqueous solution

mol wt

26 kDa

concentration

>0.1 mg/mL
>1 unit/mL

UniProt accession no.

shipped in

wet ice

storage temp.

2-8°C

Gene Information

human ... GSTM1(2944)

General description

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.

Specificity

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.

Biochem/physiol Actions

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

Warning

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

Unit Definition

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.

Physical form

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.

Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Niroshan Ramachandran et al.
Methods in molecular biology (Clifton, N.J.), 328, 1-14 (2006-06-21)
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Blanquet S, et al.
Journal of Biotechnology, 110(1), 37-49 (2004)
Ji Qiu et al.
Methods in enzymology, 500, 151-163 (2011-09-29)
Systematic study of proteins requires the availability of thousands of proteins in functional format. However, traditional recombinant protein expression and purification methods have many drawbacks for such study at the proteome level. We have developed an innovative in situ protein
Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
Smith D B and Johnson K S
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Clinical pathology in non-clinical toxicology testing
Haschek and Rousseaux's Handbook of Toxicologic Pathology, 565-594 (2013)

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