G4510
Glutathione−Agarose
lyophilized powder
Synonym(s):
Glutathione-Agarose Resin, GSH-agarose, S-linked glutathione agarose
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About This Item
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form
lyophilized powder
analyte chemical class(es)
proteins (GST)
extent of labeling
≥10 μmol per mL gel
technique(s)
immunoprecipitation (IP): suitable
protein purification: suitable
matrix
4% cross-linked beaded agarose
matrix activation
epoxy
matrix attachment
sulfur
matrix spacer
12 atoms (10 carbon)
storage temp.
−20°C
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General description
Glutathione S-transferase (GST) is a protein with a molecular weight of 26 KDa that naturally occurs in eukaryotic cells. It belongs to the family of Phase II detoxification enzymes. Glutathione-Agarose consists of glutathione attached through its sulfur to epoxy-activated 4% cross-linked beaded agarose, resulting in a 12-atom (10-carbon) spacer. It is provided as a lyophilized powder stabilized with lactose.
Application
Glutathione-Agarose has been used:
- to purify glutathione S-transferase (GST)-fused protein for generating polyclonal antibody M4P
- to incubate supernatant fractions for the purification of full-length p53 (aa 1-393) and its DNA-binding domain (aa 94-288)
- in affinity purification of the fusion protein
Affinity chromatography using glutathione-agarose permits rapid, mild, non-denaturing and highly selective purification of proteins containing glutathione binding sequences, such as Glutathione S-Transferase (GST), glutathione peroxidase and glyoxalase I.
Biochem/physiol Actions
Glutathione S-transferases (GSTs), a superfamily of multifunctional detoxification isoenzymes, have a significant role in cellular signaling. GSTs are emerging as promising therapeutic targets due to the overexpression of specific isozymes in various tumors and their potential involvement in the development of other diseases such as neurodegenerative diseases, multiple sclerosis, and asthma.
Features and Benefits
- Offers rapid, mild, non-denaturing, and highly selective purification of glutathione-binding enzymes.
- Has a shelf life of two years if stored properly desiccated at -20 °C.
- Binding capacity: 5-10 mg glutathione S-transferase per mL resin
Quantity
One g powder swells to ≥10 ml of gel
Physical form
Lyophilized powder stabilized with lactose
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Wenrong Tan et al.
PLoS genetics, 14(4), e1007336-e1007336 (2018-04-17)
Drought is a major threat to plant growth and crop productivity. The phytohormone abscisic acid (ABA) plays a critical role in plant response to drought stress. Although ABA signaling-mediated drought tolerance has been widely investigated in Arabidopsis thaliana, the feedback
Samie R Jaffrey et al.
Proceedings of the National Academy of Sciences of the United States of America, 99(5), 3199-3204 (2002-02-28)
The specificity of the reactions of nitric oxide (NO) with its neuronal targets is determined in part by the precise localizations of neuronal NO synthase (nNOS) within the cell. The targeting of nNOS is mediated by adapter proteins that interact
Magdalena M Grabowska et al.
Molecular endocrinology (Baltimore, Md.), 28(6), 949-964 (2014-05-08)
Androgen receptor (AR) action throughout prostate development and in maintenance of the prostatic epithelium is partly controlled by interactions between AR and forkhead box (FOX) transcription factors, particularly FOXA1. We sought to identity additional FOXA1 binding partners that may mediate
Hui Li et al.
Nature communications, 9(1), 2573-2573 (2018-07-04)
The dynamic maintenance of polar domains in the plasma membrane (PM) is critical for many fundamental processes, e.g., polar cell growth and growth guidance but remains poorly characterized. Rapid tip growth of Arabidopsis pollen tubes requires dynamic distribution of active
Identification, characterization, and crystal structure of the Omega class glutathione transferases.
P G Board et al.
The Journal of biological chemistry, 275(32), 24798-24806 (2000-04-28)
A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence alignment. Glutathione S-transferases (GSTs) of the new class, named Omega, exist in several mammalian species and Caenorhabditis elegans. In humans
Related Content
Investigate in vitro protein-protein interactions with pull-down assays, utilizing affinity, GST pull-down, TAP, and co-immunoprecipitation methods.
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