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G1160

Sigma-Aldrich

Monoclonal Anti-Glutathione-S-Transferase (GST) antibody produced in mouse

clone GST-2, ascites fluid

Synonyme(s) :

Mouse Anti-GST Tag

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

mouse

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

ascites fluid

Type de produit anticorps

primary antibodies

Clone

GST-2, monoclonal

Contient

15 mM sodium azide

Technique(s)

dot blot: suitable
indirect ELISA: suitable
western blot: 1:1,000 using purified recombinant GST or lysate of induced bacteria expressing recombinant GST

Isotype

IgG2b

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Description générale

Monoclonal anti-glutathione-S-transferase (GST) (mouse IgG2b isotype) is derived from the GST-2 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from a BALB/c mouse immunized with a purified recombinant GST fusion protein.GST belongs to three family of proteins distinguished as cytosolic, mitochondrial and microsomal GST. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: α, κ, μ, ω, σ, θ, π and ζ.
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. Monoclonal Anti-Glutathione-S-Transferase (GST) antibody reacts with GST from Schistosoma japonicum. Furthermore, the product identifies native as well as denatured-reduced forms of purified GST and GST fusion proteins. The antibody does not detect GST derived from rat, rabbit, porcine and bovine liver or from human placenta.

Immunogène

recombinant Glutathione-S-Transferase (GST) fusion protein.

Application

Monoclonal Anti-Glutathione-S-Transferase (GST) antibody has been used for use in western blot and ELISA. This product has also been used for dot blot.

Actions biochimiques/physiologiques

Glutathione S-transferases (GSTs) are a family of enzymes that play an important role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione.

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

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Claudia Ester et al.
BMC biochemistry, 9, 29-29 (2008-11-19)
The FF domain is conserved across all eukaryotes and usually acts as an adaptor module in RNA metabolism and transcription. Saccharomyces cerevisiae encodes two FF domain proteins, Prp40, a component of the U1 snRNP, and Ypr152c, a protein of unknown
Marie Brázdová et al.
PloS one, 8(3), e59567-e59567 (2013-04-05)
Hot spot mutant p53 (mutp53) proteins exert oncogenic gain-of-function activities. Binding of mutp53 to DNA is assumed to be involved in mutp53-mediated repression or activation of several mutp53 target genes. To investigate the importance of DNA topology on mutp53-DNA recognition
Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily.
Sheehan D, et al.
The Biochemical Journal, 360(1), 1-16 (2001)
Björn Titz et al.
Journal of bacteriology, 188(21), 7700-7706 (2006-08-29)
TP0658 (FliW) and its orthologs, conserved proteins of unknown function in Treponema pallidum and other species, interact with a C-terminal region of flagellin (FlaB1-3 in T. pallidum; FliC in most other species). Mutants of orthologs in Bacillus subtilis and Campylobacter
Jing-Xiang Wu et al.
Nature communications, 6, 8953-8953 (2015-12-03)
The SAD/BRSK kinases participate in various important life processes, including neural development, cell cycle and energy metabolism. Like other members of the AMPK family, SAD contains an N-terminal kinase domain followed by the characteristic UBA and KA1 domains. Here we

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