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G4510

Millipore

Glutathione−Agarose

lyophilized powder

Synonym(s):

Glutathione-Agarose Resin, GSH-agarose, S-linked glutathione agarose

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About This Item

MDL number:
UNSPSC Code:
41106500
NACRES:
NA.56

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)

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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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
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
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
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
Samir Sayed et al.
Diabetes, 58(6), 1419-1427 (2009-04-02)
Heterozygous activating mutations of glucokinase have been reported to cause hypoglycemia attributable to hyperinsulinism in a limited number of families. We report three children with de novo glucokinase hyperinsulinism mutations who displayed a spectrum of clinical phenotypes corresponding to marked

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