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A7340

Sigma-Aldrich

Anti-Glutathione-S-Transferase (GST)–Peroxidase Conjugate antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Anti-Glutathione-S-Transferase, Anti-GST

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.46

biological source

rabbit

conjugate

peroxidase conjugate

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 27.5 kDa

technique(s)

direct ELISA: 1:10,000
western blot: 1:10,000 using lysates of Escherichia coli induced to express recombinant GST

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

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General description

Glutathione-S-Transferase (GST) belongs to a family of Phase II detoxification enzymes which are involved in catalyzing the conjugation of glutathione (GSH) with many exogenous and endogenous electrophilic substances. GST is of two kinds- membrane-bound microsomal and cytosolic. The cytosolic GSTs are made of six classes: α, μ, ω, π, θ, and ζ.
The antibody is specific for native as well as denatured-reduced forms of glutathione-S-transferase from Schistosoma japonicum. Anti-GST may be used in various immunoassays to identify the expression of GST fusion proteins.

Specificity

Recombinant target proteins are often expressed as a fusion product with Glutathione-S-Transferase (GST) tags using various expression vector constructs. Thus, antibodies directed against the GST tags of the recombinant constructs can facilitate the purification and study of target proteins.

Immunogen

recombinant GST from Schistosoma japonicum expressed in E. coli.

Application

Anti-Glutathione-S-Transferase (GST)-Peroxidase Conjugate antibody has been used in
  • immunoblotting
  • affinity pull-down assay
  • western blotting
  • enzyme linked immunosorbent assay (ELISA)

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

Biochem/physiol Actions

Glutathione-S-Transferase (GST) are involved in protecting cellular macromolecules from the reactive electrophiles. The μ and π transferases regulate the mitogen-activated protein (MAP) kinase pathway. GSTs help in building up cellular resistance against microbial antibiotic, herbicides, insecticides, chemotherapy agents and drugs.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 0.05% MIT.

Preparation Note

Prepared by the two-step glutaraldehyde method described by Avrameas, S., et al., Scand. J. Immunol., 8, Suppl. 7, 7 (1978).

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

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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The availability of an annotated genome sequence for the yeast Saccharomyces cerevisiae has made possible the proteome-scale study of protein function and protein-protein interactions. These studies rely on availability of cloned open reading frame (ORF) collections that can be used
Activating transcription factor 6 derepression mediates neuroprotection in Huntington disease
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The Journal of Clinical Investigation, 126(2), 627-638 (2016)
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Nature communications, 9(1), 4549-4549 (2018-11-02)
Src homology 2 (SH2) domains play a critical role in signal transduction in mammalian cells by binding to phosphorylated Tyr (pTyr). Apart from a few isolated cases in viruses, no functional SH2 domain has been identified to date in prokaryotes.
G Garrait et al.
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An innovative "biodrug" concept based on oral administration of living recombinant microorganisms as a vehicle to deliver active compounds directly into the digestive tract has recently been developed. To validate this concept, we studied a recombinant Saccharomyces cerevisiae strain in

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