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Reduced Glutathione

Reduced glutathione (GSH) is a tripeptide antioxidant found in all mammalian cells.
It plays a crucial role in protecting cells from oxidative damage, detoxifying harmful compounds, and supporting various metabolic processes.
PubCompare.ai's AI-driven tool can help researchers locate protocols from literature, preprints, and patents, and use advanced comparisons to identify the best GSH protocols and products for reproducibility and accuracy.
Unleash the power of reduced glutathione in your research with PubCompare.ai's optimization solutions.

Most cited protocols related to «Reduced Glutathione»

1
Maintaining Healthy Adult Brain Slices
The adult brain slice method we have described has been successfully implemented in a variety of experimental contexts for analysis of diverse brain regions and cell types. However, we would encourage adopters to view this method as a work in progress, and we believe there is still substantial room for systematic improvement. As a case in point, we have observed that mature adult brain slices experience high levels of oxidative stress due in large part to rapid depletion of cellular antioxidants including ascorbate and reduced glutathione (GSH). This can lead to lipid peroxidation, neuronal membrane rigidity, and tissue deterioration. There appears to be a nonuniform susceptibility to this form of oxidative damage, for example, CA1 and CA3 pyramidal neurons are particularly vulnerable, making patch clamp recording of these cells difficult in brain slices from adult and aging animals in spite of the protective recovery method.
The specific restoration of intracellular pools of neuronal GSH (e.g. supplementation with the cell-permeable GSH-ethyl ester) is highly effective at curbing deterioration and prolonging slice viability under these circumstances. Thus, we have been able to further improve the NMDG recovery method by devising strategies for stimulating de novo synthesis of glutathione during acute brain slice preparation and incubation. This is most readily accomplished by adding the inexpensive GSH precursor N-acetyl-L-cysteine (NAC, 5–12 mM) to the NMDG aCSF and HEPES holding aCSF formulas, but not the recording aCSF (seeNote 14). NAC is cell-permeable and has been shown to specifically increase neuronal glutathione levels in brain tissue (26 (link)). Within 1–2 hours of slice preparation we are able to observe notable improvements in the general appearance of neurons and in the ease of patch clamp recording, and the slices are able to be maintained in a healthy state for extended time periods.
Although these more advanced methods are not absolutely required for successful adult brain slice patch clamp recordings (as demonstrated by the specific application we have described in this chapter), we include this information in hopes of providing more options to extend the versatility of our method for particularly challenging applications. Glutathione restoration is highly effective at maintaining healthy brain slices but may not be appropriate in every experimental context, e.g. investigations focusing on oxidative stress in the aging brain. On the other hand, without implementing the NMDG protective recovery method together with glutathione restoration strategy, targeted patch clamp analysis in brain slices from very old animals is prohibitively challenging.
Ting J.T., Daigle T.L., Chen Q, & Feng G. (2014). Acute brain slice methods for adult and aging animals: application of targeted patch clampanalysis and optogenetics. Methods in molecular biology (Clifton, N.J.), 1183, 221-242.
Publication 2014
Acetylcysteine Adult Anabolism Animals Antioxidants Brain Cells Diet, Formula Esters Gastrin-Secreting Cells Glutathione HEPES Lipid Peroxidation Muscle Rigidity Neurons Oxidative Damage Oxidative Stress Permeability Protoplasm Pyramidal Cells Reduced Glutathione Susceptibility, Disease Tissue, Membrane Tissues
2
Engineering Redox-Sensitive RoGFP Sensors
The RoGFP protein contains two engineered cysteine thiols, as first described by Remington et al. (RoGFP2) 11 (link). The cDNA encoding the protein was created by introducing four mutations in the mammalian GFP expression vector (pEGFP-N1) (C48S, Q80R, S147C, and Q204C) using a QuikChange Multi Site-directed mutagenesis kit (Strategene). The RoGFP construct was ligated into the VQ Ad5CMV K-NpA adenoviral shuttle vector between the KpnI and NotI sites; after sequencing and amplification this plasmid was used to generate a recombinant adenovirus to permit widespread expression in our cells (ViraQuest Inc., North Liberty, IA). The resulting redox-sensitive protein has excitation maxima at 400 and 484 nm, with emission at 525 nm. In response to changes in redox conditions, RoGFP exhibits reciprocal changes in intensity at the two excitation maxima 12 (link), and its ratiometric characteristics render it insensitive to expression levels 13 (link)-15 (link). Although RoGFP’s fluorescence behavior is relatively independent of pH and it does not respond to authentic nitric oxide (NO), reduced NADH, or the antioxidant N-acetyl-L-cysteine (NAC), its spectrum is slightly affected by reduced glutathione (GSH) possibly due to thiol-disulfide exchange (Online Figures I and II).
RoGFP was expressed in the mitochondrial matrix (Mito-RoGFP) by appending a 48 bp region encoding the mitochondrial targeting sequence from cytochrome oxidase subunit IV, at the 5′ end of the coding sequence. This construct was then ligated into the VQ Ad5CMV K-NpA plasmid between the KpnI and NotI sites, and used to generate an adenoviral vector. RoGFP was targeted to the mitochondrial inter-membrane space (IMS-RoGFP) by appending it to glycerol phosphate dehydrogenase (GPD). A cDNA construct encoding GPD, an integral protein of the inner mitochondrial membrane whose C-terminus protrudes into the inter-membrane space 17 (link), was ligated in-frame with cDNA encoding RoGFP 17 (link). The corresponding polypeptide includes amino acids 1–626 of GPD, with RoGFP at the carboxy terminus. This method has been used previously to express YFP in the inter-membrane space 18 (link). (See Online Supplemental Material for characterization of the RoGFP sensors and experimental protocols).
Waypa G.B., Marks J.D., Guzy R., Mungai P.T., Schriewer J., Dokic D, & Schumacker P.T. (2009). HYPOXIA TRIGGERS SUBCELLULAR COMPARTMENTAL REDOX SIGNALING IN VASCULAR SMOOTH MUSCLE CELLS. Circulation research, 106(3), 526-535.
Publication 2009
Acetylcysteine Adenoviruses Adenovirus Vaccine Amino Acids Antioxidants Cells Cloning Vectors Cysteine Cytochrome-c Oxidase Subunit IV Disulfides DNA, Complementary Fluorescence glycerol-1-phosphate dehydrogenase Glycerol-3-Phosphate Dehydrogenase Integral Membrane Proteins Mammals Mitochondria Mitochondrial Membrane, Inner Mitochondrial Membranes Mitomycin Mutagenesis, Site-Directed Mutation NADH Open Reading Frames Oxidation-Reduction Oxide, Nitric Plasmids Polypeptides Proteins Reading Frames Reduced Glutathione Shuttle Vectors Sulfhydryl Compounds Tissue, Membrane
3
Recombinant Hp1018/19Δsp Protein Purification
The construct Hp1018/19Δsp was amplified from genomic DNA of H. pylori strain 26695 using the primers 5′-aaggatccggcaatatccaaatccagagcatg-3′ and 5′-aagaattcgacccacccctatcatttcacc-3′ with Pfx DNA polymerase in supplied buffer with 2× PCR Enhancer (Invitrogen). The amplified BamH1/EcoR1 flanked PCR product was then ligated into the pGEM-T Easy plasmid (Promega), subcloned into the pGEX-6P-1 plasmid DNA (GE Healthcare Life Sciences) and transformed in E. coli BL21. The construction of the protease-inactive Hp1018/19ΔspS205A protein, serine 205 was mutated to alanine using the QuikChange® Lightning Site-Directed Mutagenesis Kit (Stratagene) according to the manufacturer's instructions. For heterologous overexpression and purification of GST-Hp1018/19Δsp, transformed E. coli was grown in 500 ml TB medium to an OD550 of 0.6 and the expression was induced by the addition of 0.1 mM isopropylthiogalactosid (IPTG). The bacterial culture was pelleted at 4000×g for 30 minutes and lysed in 25 ml PBS by sonification. The lysate was cleared by centrifugation and the supernatant was incubated with glutathione sepharose (GE Healthcare Life Sciences) at 4°C over night. The fusion protein was either eluted with 10 mM reduced glutathione for 10 minutes at room temperature or cleaved with 180 U Prescission Protease for 16 h at 4°C (GE Healthcare Life Sciences). Elution and cleavage products were analyzed by SDS PAGE and zymography.
Löwer M., Weydig C., Metzler D., Reuter A., Starzinski-Powitz A., Wessler S, & Schneider G. (2008). Prediction of Extracellular Proteases of the Human Pathogen Helicobacter pylori Reveals Proteolytic Activity of the Hp1018/19 Protein HtrA. PLoS ONE, 3(10), e3510.
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Publication 2008
Alanine Bacteria Buffers Centrifugation Cytokinesis DNA-Directed DNA Polymerase Escherichia coli Genome Glutathione Helicobacter pylori Mutagenesis, Site-Directed Oligonucleotide Primers Peptide Hydrolases Plasmids Promega prostaglandin M Proteins Reduced Glutathione SDS-PAGE Sepharose Serine Strains
4
Antioxidant Enzyme Activity in Tissues
After 3-NPA (12.5 mg/kg) treatment for seven days, different tissues (ovary, brain, spleen, liver and kidney) were collected. Separately, tissue from each of the five sampled organs (ovary, brain, spleen, liver and kidney) was homogenized in cold saline to prepare for the assay for activity of antioxidant enzymes. The activities of three enzymes—T-SOD, GPx and CAT—were determined using commercial kits (Nanjing Jiancheng Bioengineering Institute, Nanjing, China). (1) T-SOD activity was assayed using the xanthine/xanthine oxidase method based on the production of O2− anions. (2) GPX activity was estimated based on its catalyzation by the oxidation of reduced glutathione in the presence of cumene hydroperoxide. The generation of nicotinamide adenine dinucleotide phosphate was measured spectrophotometrically at 340 nm. (3) CAT activity was measured by analyzing the rate at which it caused the decomposition of H2O2 at 240 nm, the substrate of the enzyme contained in various tissue samples. Activities of T-SOD and GPX are expressed as units per milligrams of protein (U/mg protein). The activity of CAT is expressed as (U/g protein).
Zhang J.Q., Shen M., Zhu C.C., Yu F.X., Liu Z.Q., Ally N., Sun S.C., Li K, & Liu H.L. (2014). 3-Nitropropionic Acid Induces Ovarian Oxidative Stress and Impairs Follicle in Mouse. PLoS ONE, 9(2), e86589.
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Publication 2014
Anions Antioxidant Activity Brain Cold Temperature cumene hydroperoxide enzyme activity Enzymes GTP-Binding Proteins Kidney Liver NADP Ovary Peroxide, Hydrogen Proteins Reduced Glutathione Saline Solution Spleen Tissues Xanthine Oxidase
5
Metabolic Profiling of Detached Mammary Cells
MCF-10A cells and their variants were all cultured as described on http://brugge.med.harvard.edu/. Other cell lines were cultured as described in the supplementary information. All assays on ECM detached cells were carried out 24 hours after plating on poly-HEMA coated plates unless otherwise noted. ATP assays were conducted using either the ATPlite assay (PerkinElmer, Waltham, MA), the ATP determination kit (Invitrogen, Carlsbad, CA), or the ATP/ADP Ratio Assay Kit (BioAssay Systems, Hayward, CA). Glucose uptake assays were performed using the Amplex Red Glucose Assay Kit (Invitrogen). ROS was measured using carboxy-H2DCF-DA in detached/attached cells and in 3D culture. To measure reduced glutathione, we used chloromethylcoumarin (CMAC, Invitrogen). FAO was measured by monitoring the release of 14CO2 after addition of 1-14C-Oleic Acid. 3D culture of mammary acini was completed according to the protocol at http://brugge.med.harvard.edu/. Native fluorescence of NAD(P)H was measured using two-photon microscopy. Soft agar assays were performed in the presence or absence of antioxidants and colony formation/size was determined using ImageJ.
Full methods and any associated references are available in the online version of the paper at www.nature.com/nature.
Schafer Z.T., Grassian A.R., Song L., Jiang Z., Gerhart-Hines Z., Irie H.Y., Gao S., Puigserver P, & Brugge J.S. (2009). Antioxidant and Oncogene Rescue of Metabolic Defects Caused by Loss of Matrix Attachment. Nature, 461(7260), 109-113.
Publication 2009
Agar Antioxidants Biological Assay Breast Cell Lines Cells Fluorescence Glucose Microscopy NADH Oleic Acid Polyhydroxyethyl Methacrylate Reduced Glutathione

Most recents protocols related to «Reduced Glutathione»

1
Quantifying Oxidative Stress Markers in Plasma
In plasma samples, the following oxidative stress markers were measured: nitrite (NO2), superoxide anion radical (O2−), hydrogen peroxide (H2O2), and the index of lipid peroxidation (measured as TBARS – thiobarbituric acid reactive substances).
Nitric oxide decomposes rapidly to form stable metabolite nitrite/nitrate products. The nitrite level was measured and used as an index of nitric oxide (NO) production using the Griess reagent. A total of 0.5 ml of plasma was precipitated with 200 μl of 30% sulphosalicylic acid, vortexed for 30 min, and centrifuged at 3000 × g. Equal volumes of supernatant and Griess reagent containing 1% sulphanilamide in 5% phosphoric acid/0.1% naphthalene ethylenediamine dihydrochloride were added and incubated for 10 min in the dark, and the sample was measured at 543 nm. The nitrite levels were calculated using sodium nitrite as the standard [13 (link)].
The O2− concentration was measured after the reaction of nitro blue tetrazolium in Tris buffer with the plasma at 530 nm. Distilled water served as the blank [14 ].
The measurement of H2O2 is based on the oxidation of phenol red by H2O2 in a reaction catalysed by horseradish peroxidase (HRPO). Two hundred μl of plasma was precipitated with 800 ml of freshly prepared phenol red solution, followed by the addition of 10 μl of (1:20) HRPO (made ex tempore). Distilled water was used as the blank instead of the plasma sample. H2O2 was measured at 610 nm [15 (link)].
The degree of lipid peroxidation in the plasma samples was estimated by measuring TBARS using 1% thiobarbituric acid in 0.05 NaOH, incubated with the plasma at 100 °C for 15 min, and measured at 530 nm. Distilled water served as the blank [16 (link)].
The activity of the following antioxidants in the lysate was determined: reduced glutathione (GSH), catalase (CAT), and superoxide dismutase (SOD). The level of reduced glutathione was determined based on GSH oxidation with 5,5-dithiobis-6,2-nitrobenzoic acid using a method by Beutler [17 ]. The CAT activity was determined according to Aebi [18 (link)]. The lysates were diluted with distilled water (1:7 v/v) and treated with chloroform-ethanol (0.6:1 v/v) to remove haemoglobin, and then 50 μl of CAT buffer, 100 μl of sample and 1 ml of 10 mM H2O2 were added to the samples. The detection was performed at 360 nm. SOD activity was determined by the epinephrine method of Beutler [19 (link)]. Lysate (100 μl) and 1 ml carbonate buffer were mixed, and then 100 μl of epinephrine was added. The detection was performed at 470 nm.
Radoman K., Zivkovic V., Zdravkovic N., Chichkova N.V., Bolevich S, & Jakovljevic V. (2023). Effects of dandelion root on rat heart function and oxidative status. BMC Complementary Medicine and Therapies, 23, 78.
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Publication 2023
Anions Antioxidant Activity Buffers Carbonates Catalase Chloroform Epinephrine Ethanol ethylenediamine dihydrochloride Griess reagent Hemoglobin Horseradish Peroxidase Lipid Peroxidation naphthalene Nitrates Nitrites Nitrobenzoic Acids Nitroblue Tetrazolium Oxidative Stress Oxide, Nitric Peroxide, Hydrogen Phosphoric Acids Plasma Reduced Glutathione Sodium Nitrite Sulfanilamide sulfosalicylic acid Superoxide Dismutase Superoxides thiobarbituric acid Thiobarbituric Acid Reactive Substances Tromethamine
2
Expression and Purification of GST-fusion Proteins
Expression and purification were performed as above, using the strain E. coli BL21 carrying either carrying pGEX4T3_stop or pGEX4T3_YgfB. Differing from above, the expression was carried out at 25 °C. For resuspension and lysis of the bacterial pellet, GST-A buffer (50 mM Tris, 150 mM NaCl, 1 mM DTT, pH 7.5) supplemented with lysozyme, Triton X-100, DNase and protease inhibitor was used. For purification, a GSTrap™ HP 1 ml column (Cytiva) connected to a peristaltic pump was used. After loading the column and collecting the flow through the column was washed using GST-A buffer and the protein eluted using GST-B-buffer (50 mM Tris, 150 mM NaCl, 10 mM reduced glutathione, pH 8). After column regeneration, the flow through was loaded on the column once again and also washed and eluted. The obtained eluate fractions were pooled and dialysed against 10 liter of PBS pH 7.4 and 0.5 mM DTT using a ZelluTrans (Roth) dialysis tube with a 3.4 kDa cutoff and frozen in dialysis buffer. Analysis by SDS-PAGE and protein storage was done as described above.
Eggers O., Renschler F.A., Michalek L.A., Wackler N., Walter E., Smollich F., Klein K., Sonnabend M.S., Egle V., Angelov A., Engesser C., Borisova M., Mayer C., Schütz M, & Bohn E. (2023). YgfB increases β-lactam resistance in Pseudomonas aeruginosa by counteracting AlpA-mediated ampDh3 expression. Communications Biology, 6, 254.
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Publication 2023
Bacteria Buffers Deoxyribonucleases Dialysis Escherichia coli Freezing Muramidase Peristalsis Protease Inhibitors Proteins Reduced Glutathione Regeneration SDS-PAGE Sodium Chloride Strains Triton X-100 Tromethamine
3
Quantifying Oxidative Stress Biomarkers
A 0.30–0.45 g weighted pieces of tissue samples collected were homogenized in 50 mM phosphate buffer (pH 7.4) and centrifuged for 10 min at 3000 rpm at 4 °C and the supernatants were then stored at −20 °C until used for determination of malondialdehyde (MDA), reduced glutathione (GSH) and antioxidant enzymes CAT and SOD in accordance to following protocols described by Ohkawa et al.63 (link), Beutter et al.64 (link), Aebi65 (link), and Nishikimi et al.66 (link).
Ghebryal L.N., Noshy M.M., El-Ghor A.A, & Eissa S.M. (2023). Comparative analysis of Acomys cahirinus and Mus musculus responses to genotoxicity, oxidative stress, and inflammation. Scientific Reports, 13, 3989.
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Publication 2023
Antioxidants Buffers Enzymes Malondialdehyde Phosphates Reduced Glutathione Tissues
4
Glutathione-Mediated Detoxification Assay
1-chloro-2, 4-dinitrobenzene (CDNB), phenylmethylsulfonylfluoride (PMSF), reduced glutathione (GSH), glutathione sepharose 4 fast flow, sephacryl S-300, cumene hydroperoxide, p-hydroxymercuribenzoate, lithocholic acid, hematin, p-chloromercuribenzoic acid (pCMB), N-p-tosyl-l-phenylalanine chloromethyl ketone (TPCK), iodoacetamide, gel filtration molecular weight markers, and triphenyltin chloride were purchased from Sigma Chemical Co. All other chemicals were of analytical grade.
Masoud H.M., Helmy M.S., Darwish D.A, & Ibrahim M.A. (2023). Purification, characterization, and enzyme kinetics of a glutathione S transferase from larvae of the camel tick Hyalomma dromedarii. Journal of Genetic Engineering & Biotechnology, 21, 28.
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Publication 2023
4-hydroxymercuribenzoate Biological Markers cumene hydroperoxide Dinitrobenzenes Gel Chromatography Glutathione Hematin Iodoacetamide Ketones Lithocholic Acid p-Chloromercuribenzoic Acid Phenylalanine Reduced Glutathione Sepharose triphenyltin chloride
5
Expression and Purification of Recombinant GST-Tagged Proteins
The cDNA of human full-length SMN and truncations were inserted in pGEX-6P-1 (GE Healthcare) using BamHI and XhoI. Aromatic cage mutants were generated by site-directed mutagenesis using Pfu Turbo (Stratagene) followed by DpnI (NEB) digestion. Constructs were sequence-verified (GATC Biotech AG or Biofidal) and transformed into BL21 DE3 cells (Stratagene). BL21 cells were grown overnight with ampicillin selection at 37°C with agitation. The following day, cultures were scaled up in 250 ml LB (Sigma-Aldrich) and grown at 37°C until OD600 ∼0.6. Then, expression of recombinant GST proteins was induced with 0.2 mM IPTG for 2.5–3 h at 37°C. Cells were harvested by centrifugation and resuspended in lysis buffer (50 mM Tris, pH 7.5, 150 mM NaCl, 0.05% NP-40, supplemented Complete EDTA-free [Roche]). After a brief sonication, lysates were cleared by centrifugation and incubated with glutathione–sepharose (GE Healthcare) at 4°C on a tumbler wheel. After extensive washing, GST proteins were eluted with 10 mM reduced glutathione (Sigma-Aldrich) in 50 mM Tris, pH 8.0.
Binda O., Kimenyi Ishimwe A.B., Galloy M., Jacquet K., Corpet A., Fradet-Turcotte A., Côté J, & Lomonte P. (2023). The TUDOR domain of SMN is an H3K79me1 histone mark reader. Life Science Alliance, 6(6), e202201752.
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Publication 2023
Ampicillin Buffers Cells Centrifugation Digestion DNA, Complementary Edetic Acid Glutathione Homo sapiens Isopropyl Thiogalactoside Mutagenesis, Site-Directed Nonidet P-40 Proteins Recombinant Proteins Reduced Glutathione Sepharose Sodium Chloride Tromethamine

Top products related to «Reduced Glutathione»

1
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Reduced glutathione is a biochemical compound that serves as an antioxidant in biological systems. It plays a key role in maintaining the redox state of cells and protecting them from oxidative stress.
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Thiobarbituric acid by Merck Group
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Thiobarbituric acid is a chemical compound used in various laboratory applications. It is a white to pale yellow crystalline solid that is soluble in water and organic solvents. Thiobarbituric acid is commonly used as a reagent in analytical techniques to detect the presence of certain compounds, particularly those related to lipid peroxidation.
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Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.
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Glutathione Sepharose 4B is a chromatography resin used for the purification of proteins tagged with glutathione S-transferase (GST). It consists of the glutathione ligand covalently coupled to Sepharose 4B beads. The resin can be used to efficiently capture and purify GST-tagged proteins from complex samples.
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Reduced glutathione (GSH) is a tripeptide composed of glutamic acid, cysteine, and glycine. It is a common antioxidant found in living organisms, playing a crucial role in cellular processes. GSH functions as a reducing agent, helping to maintain the appropriate oxidation-reduction state within cells.
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L-glutathione reduced is a laboratory reagent used in various biochemical and analytical applications. It is the reduced form of the antioxidant glutathione, which plays a crucial role in cellular processes. This product is commonly used as a reducing agent, cofactor, and protective agent in cell culture, enzymatic assays, and other research procedures. The specific details and intended use of this product should be obtained from the manufacturer or relevant scientific literature.
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Glutathione-Sepharose beads are a chromatography resin designed for the purification of glutathione-S-transferase (GST) fusion proteins. The beads consist of cross-linked agarose beads with covalently coupled glutathione, which can selectively bind to GST-tagged proteins. This allows for the isolation and enrichment of GST-fusion proteins from complex mixtures.
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5 5 dithiobis 2 nitrobenzoic acid by Merck Group
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More about "Reduced Glutathione"

Reduced glutathione (GSH) is a crucial tripeptide antioxidant found in all mammalian cells.
It plays a vital role in protecting cells from oxidative damage, detoxifying harmful compunds, and supporting various metabolic processes.
GSH is a key player in maintaining cellular homeostasis and preventing oxidative stress.
Closely related to GSH is the compound thiobarbituric acid, which is often used in assays to measure lipid peroxidation and oxidative stress.
Bovine serum albumin is another important biomolecule that can be used in conjunction with GSH-related experiments, serving as a protein standard.
The Glutathione Sepharose 4B resin is a valuable tool for purifying and isolating GSH-dependent enzymes and proteins.
L-glutathione reduced is the primary, biologically active form of GSH, while trichloroacetic acid is commonly used to precipitate proteins during GSH quantification.
Glutathione-Sepharose beads provide a convenient way to immobilize GSH for affinity chromatography, while 5,5'-dithiobis(2-nitrobenzoic acid) (also known as Ellman's reagent) is used to colorimetrically detect and quantify thiol groups, including those found in GSH.
Researchers can leverage the power of reduced glutathione in their studies by utilizing PubCompare.ai's AI-driven optimization tool.
This tool can help locate the best protocols from literature, preprints, and patents, and provide advanced comparisons to identify the most reproducible and accurate GSH-related methods and products.
Unlock the full potential of GSH in your research with PubCompare.ai's innovative solutions.