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Principaux documents

G7781

Sigma-Aldrich

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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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

IgG fraction of antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Conditionnement

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

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

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Description générale

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.

Immunogène

recombinant GST from Schistosoma japonicum expressed in E. coli.

Application

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

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

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


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Consulter la Bibliothèque de documents

Glutathione S-transferase polymorphisms and their biological consequences
Hayes JD and Strange RC
Pharmacology, 61(3), 154-166 (2000)
Dennis G Drescher et al.
Methods in molecular biology (Clifton, N.J.), 493, 323-343 (2008-10-08)
Surface plasmon resonance is an optical technique utilized for detecting molecular interactions. Binding of a mobile molecule (analyte) to a molecule immobilized on a thin metal film (ligand) changes the refractive index of the film. The angle of extinction of
Analysis of protein-ligand interactions by fluorescence polarization
Rossi AM and TaylorCW
Nature Protocols, 6(3), 365-365 (2011)
Laura Castaño-Miquel et al.
The Biochemical journal, 436(3), 581-590 (2011-03-19)
Protein modification by SUMO (small ubiquitin-related modifier) has emerged as an essential regulatory mechanism in eukaryotes. Even though the molecular mechanisms of SUMO conjugation/deconjugation are conserved, the number of SUMO machinery components and their degree of conservation are specific to
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)

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