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Merck
CN

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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20 μG
CN¥3,096.05
50 μG
CN¥5,521.21

CN¥3,096.05


Estimated to ship onJuly 21, 2025Details


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20 μG
CN¥3,096.05
50 μG
CN¥5,521.21

About This Item

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

CN¥3,096.05


Estimated to ship onJuly 21, 2025Details


Request a Bulk Order

recombinant

expressed in E. coli

grade

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)

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esiRNA cDNA target sequence

GACCAGGTGGTCCTGTCCTACGGGGGCCTGCGCGGGGCCGTGGCCTTTGCCCTGGTGGTGCTTCTGGATGGAGACAAGGTCAAGGAGAAGAACCTGTTCGTCAGCACCACCATCATCGTAGTGTTCTTCACCGTCATCTTCCAGGGCCTGACCATCAAGCCTCTGGTGCAGTGGCTGAAGGTGAAGAGGAGCGAGCACCGGGAACCTCGGCTCAACGAGAAGCTGCACGGGCGCGCTTTCGACCACATCCTCTCGGCCATCGAGGACATATCCGGACAGATCGGGCACAATTATCTCAGAGACAAGTGGTCCCACTTCGACAGGAAGTTCCTCAGCAGGGTCCTCATGAGACGGTCGGCCCAGAAGTCTCGAGACCGGATCCTGAATGTCTTCCACGAGCTG

esiRNA cDNA target sequence

CACCACTGGAACTGGACCTTCGTCATCAGCACCCTGCTCTTCTGCCTCATCGCCCGCGTGCTGGGGGTGCTGGGCCTGACCTGGTTCATCAACAAGTTCCGTATCGTGAAGCTGACCCCCAAGGACCAGTTCATCATCGCCTATGGGGGCCTGCGAGGGGCCATCGCCTTCTCTCTGGGCTACCTCCTGGACAAGAAGCACTTCCCCATGTGTGACCTGTTCCTCACTGCCATCATCACTGTCATCTTCTTCACCGTCTTTGTGCAGGGCATGACCATTCGGCCCCTGGTAGACCTGTTGGCTGTGAAGAAAAAGCAAGAGACGAAGCGCTCCATCAACGAAGAGATCCACACACAGTTCCTGGACCACCTTCTGACAGGCATCGAAGACATCTGTGGCCACTACGGTCACCACCACTG

esiRNA cDNA target sequence

TTCTCCTTTCCTGGGGAACTTCTGATGAGGATGTTACAGATGCTGGTCTTACCACTTATCATCTCCAGTCTTGTCACAGGAATGGCGGCGCTAGATAGTAAGGCATCAGGGAAGATGGGAATGCGAGCTGTAGTCTATTATATGACTACCACCATCATTGCTGTGGTGATTGGCATAATCATTGTCATCATCATCCATCCTGGGAAGGGCACAAAGGAAAACATGCACAGAGAAGGCAAAATTGTACGAGTGACAGCTGCAGATGCCTTCCTGGACTTGATCAGGAACATGTTCCCTCCAAATCTGGTAGAAGCCTGCTTTAAACAGTTTAAAACCAACTATGAGAAGAGAAGCTTTAAAGTGCCCATCCAGGCCAACGAAACGCTTGTGGGTGCTGTGATAAACAATGTGTCTGAGGCCATGGAGACTCT

esiRNA cDNA target sequence

TGGCAAGATCAACAGCGTAGAGCAGAATGATATGCTACGGAAGGTAACATTCGATCCAGAAGTATTTTTCAACATTCTTCTGCCTCCAATTATTTTTCATGCTGGATACAGCTTAAAGAAGAGACACTTTTTCAGAAATCTTGGATCTATACTGGCCTATGCCTTCTTGGGGACTGCTGTTTCATGCTTCATTATTGGAAATCTCATGTATGGTGTGGTGAAGCTCATGAAGATTATGGGACAGCTCTCAGATAAATTTTACTACACAGATTGTCTCTTTTTTGGAGCAATCATCTCTGCCACTGACCCAGTGACTGTGCTGGCGATATTTAATGAATTGCATGCAGACGTGGATCTTTACGCACTTCTTTTTGGAGAGAGCGTCCTAAATGATGCTGTTGCCATTGTACTGTCCTCGTCTATTGTTGCCTACCAGCCAGCGGGACTGAACACTCACGCCTTTGA

product line

MISSION®

product line

MISSION®

product line

MISSION®

product line

MISSION®

Gene Information

human ... SLC9A3(6550), SLC9A3(6550)

Gene Information

human ... SLC9A1(6548), SLC9A1(6548)

Gene Information

human ... SLC1A3(6507), SLC1A3(6507)

Gene Information

human ... SLC9A7(84679), SLC9A7(84679)

Ensembl | human accession no.

ENSG00000066230

Ensembl | human accession no.

ENSG00000090020

Ensembl | human accession no.

ENSG00000079215

Ensembl | human accession no.

ENSG00000065923

NCBI accession no.

NM_004174

NCBI accession no.

NM_003047

NCBI accession no.

NM_004172

NCBI accession no.

NM_032591

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

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).[1][2]
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.[3]

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

Regulatory Information

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Blanquet S, et al.
Journal of Biotechnology, 110(1), 37-49 (2004)
Niroshan Ramachandran et al.
Methods in molecular biology (Clifton, N.J.), 328, 1-14 (2006-06-21)
Protein microarrays are a miniaturized format for displaying in close spatial density hundreds or thousands of purified proteins that provide a powerful platform for the high-throughput assay of protein function. The traditional method of producing them requires the high-throughput production
Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
Smith D B and Johnson K S
Gene, 67(1), 31-40 (1988)
Clinical pathology in non-clinical toxicology testing
Haschek and Rousseaux's Handbook of Toxicologic Pathology, 565-594 (2013)
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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