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A8580

Sigma-Aldrich

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

IgG fraction of antiserum, PBS suspension

Synonyme(s) :

Anti-Glutathione-S-Transferase, Anti-GST

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

rabbit

Conjugué

agarose conjugate

Forme d'anticorps

IgG fraction of antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

PBS suspension

Poids mol.

antigen 27.5 kDa

Ne doit pas réagir avec

porcine, bovine, human, rabbit, rat

Technique(s)

ELISA: suitable
immunoprecipitation (IP): suitable

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... GSTP1(2950)

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Description générale

Glutathione-S-transferases (GSTs) are dimeric proteins, which belongs to phase II detoxification enzymes family. The highly polymorphic human cytosolic GSTs are divided into six classes, such as, 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.

Immunogène

recombinant GST from Schistosoma japonicum expressed in E. coli.

Application

Immunoprecipitation was performed on NIH 3T3 cells transiently transfected with GST fusion proteins. IP was performed using agarose-linked rabbit anti-GST IgG with mixing for 2 hours at 4 degrees.
Rabbit Anti-Glutathione-S-Transferase (GST)-Agarose antibody can be used for ELISA, immunoaffinity purification and immunoprecipitation assays.

Actions biochimiques/physiologiques

Glutathione-S-transferases (GSTs) can catalyse the conjugation of glutathione (GSH) to various endogenous and exogenous electrophilic compounds. The π and μ classes of GSTs controls the mitogen-activated protein (MAP) kinase pathway. It can also serve as transport proteins.

Forme physique

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

Notes préparatoires

Prepared by coupling cyanogen bromide-activated agarose at 7-8 mg antibody per mL resin volume.

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)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Metabolism of xenobiotics of human environments
Progress in Molecular Biology and Translational Science, 112, 31-88 (2012)
Clinical pathology in non-clinical toxicology testing
Haschek and Rousseaux's Handbook of Toxicologic Pathology, 112(47), 565-594 (2013)
Xun Shang et al.
The Journal of biological chemistry, 282(12), 8801-8811 (2007-02-03)
p200 RhoGAP, a member of the Rho GTPase-activating protein (RhoGAP) family, was previously implicated in the regulation of neurite outgrowth through its RhoGAP activity. Here we show that ectopic expression of p200 RhoGAP stimulates fibroblast cell proliferation and cell cycle
Jessica Gagnon et al.
Epigenetics, 10(8), 677-691 (2015-06-16)
O-GlcNAcylation is a posttranslational modification catalyzed by the O-Linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) and reversed by O-GlcNAcase (OGA). Numerous transcriptional regulators, including chromatin modifying enzymes, transcription factors, and co-factors, are targeted by O-GlcNAcylation, indicating that this modification is central for
The role of glutathione-S-transferase in anti-cancer drug resistance
Townsend D M and Tew K D
Oncogene, 22(47), 7369-7369 (2003)
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