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About This Item
NACRES:
NA.46
UNSPSC Code:
12352203
Conjugate:
peroxidase conjugate
Clone:
polyclonal
Application:
ELISA (d), WB
Citations:
35
biological source
rabbit
conjugate
peroxidase conjugate
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 27.5 kDa
technique(s)
direct ELISA: 1:10,000, western blot: 1:10,000 using lysates of Escherichia coli induced to express recombinant GST
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Related Categories
General description
Glutathione-S-Transferase (GST) belongs to a family of Phase II detoxification enzymes which are involved in catalyzing the conjugation of glutathione (GSH) with many exogenous and endogenous electrophilic substances. GST is of two kinds- membrane-bound microsomal and cytosolic. The cytosolic GSTs are made of six classes: 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.
Immunogen
recombinant GST from Schistosoma japonicum expressed in E. coli.
Application
Anti-Glutathione-S-Transferase (GST)-Peroxidase Conjugate antibody has been used in
- immunoblotting
- affinity pull-down assay
- western blotting
- enzyme linked immunosorbent assay (ELISA)
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Western Blotting (1 paper)
Biochem/physiol Actions
Glutathione-S-Transferase (GST) are involved in protecting cellular macromolecules from the reactive electrophiles. The μ and π transferases regulate the mitogen-activated protein (MAP) kinase pathway. GSTs help in building up cellular resistance against microbial antibiotic, herbicides, insecticides, chemotherapy agents and drugs.
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.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 0.05% MIT.
Preparation Note
Prepared by the two-step glutaraldehyde method described by Avrameas, S., et al., Scand. J. Immunol., 8, Suppl. 7, 7 (1978).
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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signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
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The availability of an annotated genome sequence for the yeast Saccharomyces cerevisiae has made possible the proteome-scale study of protein function and protein-protein interactions. These studies rely on availability of cloned open reading frame (ORF) collections that can be used
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Naranjo J R, et al.
The Journal of Clinical Investigation, 126(2), 627-638 (2016)
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Nature communications, 9(1), 4549-4549 (2018-11-02)
Src homology 2 (SH2) domains play a critical role in signal transduction in mammalian cells by binding to phosphorylated Tyr (pTyr). Apart from a few isolated cases in viruses, no functional SH2 domain has been identified to date in prokaryotes.
G Garrait et al.
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