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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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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
Guillermo Sastre-Moreno et al.
Nucleic acids research, 42(15), 9821-9837 (2014-08-12)
7,8-Dihydro-8-oxo-deoxyguanosine (8oxodG) is a highly premutagenic DNA lesion due to its ability to mispair with adenine. Schizosaccharomyces pombe lacks homologs for relevant enzymes that repair 8oxodG, which suggests that this lesion could be persistent and must be tolerated. Here we
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)
Maria Jose Martin et al.
Nucleic acids research, 41(4), 2428-2436 (2013-01-01)
Human DNA polymerase mu (Polμ), a family X member involved in DNA repair, has both template-directed and terminal transferase (template-independent) activities. In addition to their ability to incorporate untemplated nucleotides, another similarity between Polµ and terminal deoxynucleotidyl transferase (TdT) is

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