Glutathione Ethyl Ester, Biotin Amide (BioGEE) (Glutathiolation Detection Reagent) - Special Packaging
Glutathione Ethyl Ester, Biotin Amide (BioGEE) (Glutathiolation Detection Reagent) - Special Packaging
Invitrogen™

Glutathione Ethyl Ester, Biotin Amide (BioGEE) (Glutathiolation Detection Reagent) - Special Packaging

Biotinylated glutathione ethyl ester (BioGEE) is a cell-permeant, biotinylated glutathione analog for the detection of glutathiolation. Under conditions of oxidativeRead more
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G3600010 x 100 μg
Catalog number G36000
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10 x 100 μg
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Biotinylated glutathione ethyl ester (BioGEE) is a cell-permeant, biotinylated glutathione analog for the detection of glutathiolation. Under conditions of oxidative stress, cells may transiently incorporate glutathione into proteins. Stressed cells incubated in BioGEE will also incorporate this biotinylated glutathione derivative into proteins, facilitating the identification of oxidation-sensitive proteins. Once these cells are fixed and permeabilized, you can detect glutathiolation levels with a fluorescent streptavidin conjugate using either flow cytometry or fluorescence microscopy. Proteins glutathiolated with BioGEE can also be extracted and analyzed by mass spectrometry or by Western blotting methods in conjunction with fluorophore- or enzyme-labeled streptavidin conjugates.
For Research Use Only. Not for use in diagnostic procedures.
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Quantity10 x 100 μg
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2810931Certificate of AnalysisJul 13, 2024G36000
2595618Certificate of AnalysisApr 14, 2023G36000
2413438Certificate of AnalysisDec 01, 2021G36000
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Citations & References (15)

Citations & References
Abstract
Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells.
Authors:Jessop CE, Bulleid NJ
Journal:J Biol Chem
PubMed ID:15507438
'The formation of disulfide bonds is an essential step in the folding of many glycoproteins and secretory proteins. Non-native disulfide bonds are often formed between incorrect cysteine residues, and thus the cell has dedicated a family of oxidoreductases that are thought to isomerize non-native bonds. For an oxidoreductase to be ... More
S-glutathiolation by peroxynitrite of p21ras at cysteine-118 mediates its direct activation and downstream signaling in endothelial cells.
Authors:Clavreul N, Adachi T, Pimental DR, Ido Y, Schöneich C, Cohen RA
Journal:FASEB J
PubMed ID:16415107
'The highly reactive species, peroxynitrite, is produced in endothelial cells in pathological states in which the production of superoxide anion and NO is increased. Here, we show that peroxynitrite added exogenously or generated endogenously in response to exposure to an NO donor or oxidized low-density lipoproteins (oxLDL) increases p21ras activity ... More
Detection and affinity purification of oxidant-sensitive proteins using biotinylated glutathione ethyl ester.
Authors:Sullivan DM, Levine RL, Finkel T,
Journal:Methods Enzymol
PubMed ID:12078486
'na'
Detecting oxidative post-translational modifications in proteins.
Authors:Gianazza E, Crawford J, Miller I
Journal:Amino Acids
PubMed ID:17021655
Oxidative stress induces various post-translational modifications (PTM); some are reversible in vivo via enzymatic catalysis. The present paper reviews specific procedures for the detection of oxidative PTM in proteins, most of them including electrophoresis. Main topics are carbonylated and glutathionylated proteins as well as modification of selected amino acids (Cys, ... More
Glutathione binding to the Bcl-2 homology-3 domain groove: a molecular basis for Bcl-2 antioxidant function at mitochondria.
Authors:Zimmermann AK, Loucks FA, Schroeder EK, Bouchard RJ, Tyler KL, Linseman DA,
Journal:J Biol Chem
PubMed ID:17690097
Bcl-2 protects cells against mitochondrial oxidative stress and subsequent apoptosis. However, the mechanism underlying the antioxidant function of Bcl-2 is currently unknown. Recently, Bax and several Bcl-2 homology-3 domain (BH3)-only proteins (Bid, Puma, and Noxa) have been shown to induce a pro-oxidant state at mitochondria (1-4). Given the opposing effects ... More
15 total citations

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