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G1160

Sigma-Aldrich

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

clone GST-2, ascites fluid

Synonym(s):

Mouse Anti-GST Tag

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

GST-2, monoclonal

contains

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

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

General description

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.

Immunogen

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.

Biochem/physiol Actions

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.

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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Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

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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Young C Shin et al.
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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
Daniel Spazierer et al.
Journal of cell science, 121(Pt 6), 825-833 (2008-02-21)
Epiplakin is a large (>725 kDa) cytoskeletal protein exclusively expressed in epithelial tissues. It has a unique structure, consisting entirely of plakin repeat domains (PRDs), one of the hallmarks of spectraplakin protein family members. Previous studies, including the phenotypic analyses
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)
Anna Brotcke et al.
Infection and immunity, 76(8), 3473-3480 (2008-06-19)
Francisella tularensis infects wild animals and humans to cause tularemia. This pathogen targets the cytosol of macrophages, where it replicates using the genes in the Francisella pathogenicity island (FPI). Virulence gene regulation in Francisella is complex, but transcriptional regulators MglA

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