A7340
抗グルタチオン-S-トランスフェラーゼ (GST)–ペルオキシダーゼ標識 ウサギ宿主抗体
IgG fraction of antiserum, buffered aqueous solution
別名:
抗グルタチオン-S-トランスフェラーゼ, 抗GST抗体
製品名
抗グルタチオン-S-トランスフェラーゼ (GST)–ペルオキシダーゼ標識 ウサギ宿主抗体, IgG fraction of antiserum, buffered aqueous solution
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
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General description
本抗体は、Schistosoma japonicum（日本住血吸虫）由来のグルタチオン-S-トランスフェラーゼの未変性型ならびに変性・還元型に特異的です。抗GSTは、GST融合タンパク質の発現を確認するために、様々な免疫アッセイに使用される場合があります。
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.
Immunogen
大腸菌で発現させた日本住血吸虫由来のリコンビナントGSTです。
Preparation Note
Avrameas, S., et al., Scand. J. Immunol., 8, Suppl. 7, 7 (1978)による2段階グルタルアルデヒド法で調製しています
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.
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.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 0.05% MIT.
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signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
保管分類
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Flavivirus NS3 and NS5 proteins interaction network: a high-throughput yeast two-hybrid screen
Le B M, et al.
BMC Microbiology, 11(1), 234-234 (2011)
Yanhui Hu et al.
Genome research, 17(4), 536-543 (2007-02-27)
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
Activating transcription factor 6 derepression mediates neuroprotection in Huntington disease
Naranjo J R, et al.
The Journal of Clinical Investigation, 126(2), 627-638 (2016)
Tomonori Kaneko et al.
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.
Metabolic engineering, 11(3), 148-154 (2009-04-07)
An innovative "biodrug" concept based on oral administration of living recombinant microorganisms as a vehicle to deliver active compounds directly into the digestive tract has recently been developed. To validate this concept, we studied a recombinant Saccharomyces cerevisiae strain in
関連コンテンツ
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