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Merck

G7781

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

IgG fraction of antiserum, buffered aqueous solution

Synonyme(s) :

Anti-Glutathione-S-Transferase, Anti GST Antibody - Anti-Glutathione-S-Transferase (GST) antibody produced in rabbit, Anti Gst Antibody, Anti-Gst Antibody, Gst Antibody, Anti-GST

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A propos de cet article

NACRES:
NA.46
UNSPSC Code:
12352203

Principaux documents

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Nom du produit

Anti-Glutathione-S-Transferase (GST) antibody produced in rabbit, IgG fraction of antiserum, buffered aqueous solution

biological source

rabbit

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

packaging

antibody small pack of 25 μL

technique(s)

dot blot: suitable
indirect ELISA: 1:10,000
western blot: 1:2,000 using lysates of induced Escherichia coli expressing GST

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

200

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Catégories apparentées

Application

Anti-Glutathione-S-Transferase (GST) antibody produced in rabbit has been used in immunoblotting.

Biochem/physiol Actions

Glutathione-S-transferase (GST) catalyzes the detoxication of electrophiles by glutathione conjugation. This enzyme provides protection against oxidative stress and toxic foreign chemicals. Polymorphism in GST gene is associated with the development of asthma and cutaneous basal cell carcinoma.

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.

General description

Anti-Glutathione-S-Transferase (GST) antibody produced in rabbit is specific for native as well as denatured-reduced forms of glutathione-S-transferase from Schistosoma japonicum. The soluble GST is encoded by eight different genes in humans namely, α, μ, θ, π, ζ, σ, κ and ω on chromosome 6, 1, 22, 11, 14, 4, not known and 10 respectively.
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.

Immunogen

recombinant GST from Schistosoma japonicum expressed in E. coli.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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Classe de stockage

10 - Combustible liquids

wgk

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter

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Certificats d'analyse (COA)

Lot/Batch Number
0000515671
0000515671
0000483561
0000483561
0000458355

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Glutathione S-transferase polymorphisms and their biological consequences
Hayes JD and Strange RC
Pharmacology, 61(3), 154-166 (2000)
Glutathione-S-transferase family of enzymes
Strange R, et al.
Mutation Research. Fundamental and Molecular Mechanisms of Mutagenesis, 482(1-2), 21-26 (2001)
Analysis of protein-ligand interactions by fluorescence polarization
Rossi AM and TaylorCW
Nature Protocols, 6(3), 365-365 (2011)
A novel simple extracellular leucine-rich repeat (eLRR) domain protein from rice (OsLRR1) enters the endosomal pathway and interacts with the hypersensitive-induced reaction protein 1 (OsHIR1).
Zhou L, et al.
Plant, Cell and Environment, 32(12), 1804-1820 (2009)
Nina Schroeder et al.
Journal of virology, 86(9), 4868-4882 (2012-02-22)
Mature vaccinia virus (vaccinia MV) infects a broad range of animals in vivo and cell cultures in vitro; however, the cellular receptors that determine vaccinia MV tropism and entry pathways are poorly characterized. Here, we performed quantitative proteomic analyses of
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