G5663
Glutathione S-Transferase from E. coli
recombinant, expressed in E. coli, buffered aqueous solution
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Synonym(s):
Glutathione S-alkenetransferase, Glutathione S-alkyltransferase, Glutathione S-aralkyltransferase, Glutathione S-aryltransferase, Glutathione S-epoxidetransferase, RX: Glutathione R-transferase
Recommended Products
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.
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.
wgk_germany
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
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Smith D B and Johnson K S
Gene, 67(1), 31-40 (1988)
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