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Dithioerythritol

Q: What are some common applications of Dithioerythritol?

Dithioerythritol is widely used in biochemical and molecular biology applications, such as protein purification, enzyme assays, and maintaining reducing conditions to prevent oxidation of sensitive biomolecules. It's particularly useful for preserving the activity and structure of proteins and other biomolecules during experimental procedures.

Q: How does the unique chemical structure of Dithioerythritol contribute to its functionality?

Dithioerythritol has a distinctive dithiol structure, which allows it to maintain reducing conditions and protect against oxidation of delicate biomolecules. This unique chemical feature makes Dithioerythritol a valuable reagent for preserving the integrity of proteins, enzymes, and other sensitive compounds during research and analysis.

Q: Are there different variations or types of Dithioerythritol available?

While Dithioerythritol is a specific synthetic organic compound, there may be different grades or purities available from various suppliers. Researchers should carefuly evaluate the quality and specifications of Dithioerythritol products to ensure they meet the requirements of their particular application and experimental protocols.

Q: How can PubCompare.ai help optimize the use of Dithioerythritol in research?

PubCompare.ai's AI-driven platfrom allows researchers to more efficiently screen the scientific literature for protocols involving Dithioerythritol. The platform's analysis can help identify the most effective protocols and highlight key differences in protocol effectiveness, enabling researchers to choose the best option for their specific research goals and ensure reproducibility and accuracy. This can save time and unlock new insights in Dithioerythritol-related research.

Dithioerythritol is a synthetic organic compound with the chemical formula C4H8O2S2.
It is a reducing agent commonly used in biochemical and molecular biology applications, such as protein purification and enzyme assays.
Dithioerythritol has a unique dithiol structure that allows it to maintain reducing conditions and prevent oxidation of sensitive biomolecules.
Researchers can leveragae PubCompare.ai's AI-driven platform to easily locate and compare dithioerythritol protocols from scientific literature, preprints, and patents, optimizing their research proceses and unlocking new insights.

Most cited protocols related to «Dithioerythritol»

Isolation and Analysis of Mouse Lymphocytes

Cited 18 times

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Publication 2015

alpha HML-1 Antibodies Bicarbonates BLOOD Buffers CD44 protein, human Cells Cervix Uteri Collagenase, Clostridium histolyticum Dithioerythritol Enzymes Female Reproductive System Flow Cytometry Hemoglobin, Sickle HEPES Hyperostosis, Diffuse Idiopathic Skeletal Intestines Intestines, Small isolation Kidney Lamina Propria Large Intestine Liver Lung Lymphocyte Matrix Metalloproteinase 2 Mucus Mus Needles Nodes, Lymph Nylons Pancreas Passive Immunization Percoll Polystyrenes Salivary Glands Spleen Stomach Streptavidin Syringes Thymus Plant Tissues Uterine Cornua Vagina

Isolation of Ribosomes from E. coli Strains

Cited 18 times

A fresh O/N culture of E. coli JE28 was used to inoculate 1 l. LB with 50 µg/ml kanamycin and grown with aeration at 37°C. At A₆₀₀ 1.0, the culture was slowly cooled to 4°C to produce run-off ribosome and harvested by centrifugation at 4000 rpm for 30 min. The cell-pellet was resuspended in lysis buffer (20 mM Tris–HCl pH 7.6, 10 mM MgCl₂, 150 mM KCl, 30 mM NH₄Cl and PMSF protease inhibitor 200 µl/l) with lysozyme (0.5 mg/ml) and DNAse I (10 µg/ml) and further lysed using a French Press or sonicator (for smaller cell pellets <2–3 g). The lysate was clarified by centrifuging twice at 18 000 rpm at 4°C, 20 min each. The cleared lysate was divided in half. From one-half 70S ribosome was purified in the conventional method and the affinity-purification method was employed with the other half. In parallel, wild-type ribosome was also purified from the parent strain MG1655 in the conventional way for comparison.
For affinity purification, a HisTrap^TMHP column (Ni²⁺–sepharose pre-packed, 5 ml, GE Healthcare) was connected to an ÄKTA prime chromatography system (GE Healthcare) equilibrated with the lysis buffer. After loading the lysate, the column was washed with 5 mM imidazole until A₂₆₀ reached the baseline. The tetra-(His)₆-tagged ribosomes were then eluted with 150 mM imidazole, pooled immediately and dialyzed 4 × for 10 min in 250 ml lysis buffer to remove the imidazole. Furthermore, the ribosomes were concentrated by centrifugation at 150 000 × g for 2 h at 4°C, resuspended in 1× polymix buffer containing 5 mM ammonium chloride, 95 mM potassium chloride, 0.5 mM calcium chloride, 8 mM putrescine, 1 mM spermidine, 5 mM potassium phosphate and 1 mM dithioerythritol (23 (link)) and shock-frozen in liquid nitrogen for storage or dissolved in the overlay buffer (20 mM Tris–HCl pH 7.6, 60 mM NH₄Cl, 5.25 mM Mg acetate, 0.25 mM EDTA and 3 mM 2-mercaptoethanol) for sucrose gradient analysis. As a control, lysate from wild-type E. coli MG1655 was applied to the same column and was treated accordingly.
For purifying JE28 and MG1655 ribosomes in the conventional ultracentrifugation method (24 (link)), the cleared lysate was layered on top of equal volume of 30% w/v sucrose cushion made in a buffer containing 20 mM Tris–HCl pH 7.6, 500 mM NH₄Cl, 10.5 mM Mg acetate, 0.5 mM EDTA, and 7 mM 2-mercaptoethanol and centrifuged at 100 000 × g for 16 h at 4°C. This step was repeated twice and in between the ribosome pellet was gently rinsed with the same buffer. Then the pellet was dissolved in 1× polymix buffer for storage or in the overlay buffer for sucrose gradient analysis as in case of the affinity-purified ones.

Ederth J., Mandava C.S., Dasgupta S, & Sanyal S. (2008). A single-step method for purification of active His-tagged ribosomes from a genetically engineered Escherichia coli. Nucleic Acids Research, 37(2), e15.

Publication 2008

2-Mercaptoethanol Acetate Buffers Calcium chloride Cells Centrifugation Chloride, Ammonium Chromatography Chromatography, Affinity Deoxyribonuclease I Dithioerythritol Edetic Acid Escherichia coli Freezing imidazole Kanamycin Magnesium Chloride Muramidase Nitrogen Parent Pellets, Drug Potassium Chloride potassium phosphate Protease Inhibitors Putrescine Ribosomes Sepharose Shock Spermidine Strains Sucrose Tetragonopterus Tromethamine Ultracentrifugation

Isolation of Lymphocyte Subsets

Cited 8 times

For isolation of SI IEL, the small intestine was removed, Peyer's Patches were excised, and the intestine was cut longitudinally and then laterally into 1cm pieces. Gut pieces and stomachs were incubated with 15.4mg/ml dithioerythritol in 10% 1xHBSS/Hepes Bicarbonate (30 min at 37°C, stirring at 200rpm) to remove IEL. For LPL isolation, gut and stomach pieces were further treated with 100U/ml Type I Collagenase (Worthington) in 5% RPMI 1640/2mM MgCl₂/2mM CaCl₂ (45 min at 37°C, stirring at 200rpm). Brains, pancreata, hearts, and kidneys were removed and cut into small pieces prior to treatment with 100U/ml Type I Collagenase (Worthington) in 5% RPMI 1640/2mM MgCl₂/2mM CaCl₂ (45 min at 37°C, stirring at 200rpm). For isolation of FRT, the uterine horns, cervix, and vaginal tissue were resected and cut into small pieces prior to treatment with 100U/ml Type IV Collagenase (Sigma) 5% RPMI 1640/2mM MgCl₂/2mM CaCl₂ (45 min at 37°C, stirring at 200rpm). Lymphocytes from intestine, stomach, brain, and FRT were purified on a 44/67% Percoll gradient (800xg at 23°C for 20 min).

Casey K.A., Fraser K.A., Schenkel J.M., Moran A., Abt M.C., Beura L.K., Lucas P.J., Artis D., Wherry E.J., Hogquist K., Vezys V, & Masopust D. (2012). Antigen independent differentiation and maintenance of effector-like resident memory T cells in tissues. Journal of Immunology (Baltimore, Md. : 1950), 188(10), 4866-4875.

Publication 2012

Bicarbonates Brain Cervix Uteri Collagenase, Clostridium histolyticum Dithioerythritol Heart HEPES Intestines Intestines, Small isolation Kidney Lymphocyte Magnesium Chloride Matrix Metalloproteinase 2 Pancreas Percoll Stomach Tissues Uterine Cornua Vagina

Discriminating Tissue-Resident CD8 T Cells

Cited 7 times

To discriminate between CD8 T cells in tissue parenchyma versus tissue vasculature, i.v. injected Ab was used as previously described (28 (link)). Briefly, 3μg of anti-CD8α Ab (53-6.7, Biolegend, San Diego, CA) was injected i.v. and allowed to circulate for three minutes prior to mouse sacrifice.
Organs were harvested and digested as previously described (29 (link)). For isolation of small intestinal intraepithelial lymphocytes (IEL), Peyer’s patches were removed, the small intestine was cut longitudinally and then laterally into small pieces. Pieces were incubated for 30 minutes with stirring at 37°C with 0.154mg/mL dithioerythritol (Sigma-Aldrich, St. Louis, MO) in 10% HBSS/HEPES. Female reproductive tract (FRT), lung and salivary gland (SG) tissues were cut into small pieces in RPMI 1640 containing 5% FBS, 2 mM MgCl₂, 2 mM CaCl₂ and 0.5mg/mL type IV collagenase for FRT (Sigma-Aldrich, St. Louis, MO) or 100 U/mL type I collagenase for lung and SG (Worthington, Lakewood, NJ) and incubated for 1 hr at 37°C with stirring. After enzymatic digestion, the remaining tissue pieces were mechanically disrupted using a gentleMACs dissociator (Miltenyi Biotec, San Diego, CA). The liver was mechanically dissociated by pushing the tissue through a 70μm-cell strainer. Single cell suspensions of IEL, FRT, lung, liver and SG were further separated using a 44/67% Percoll (GE Healthcare Life Sciences, Pittsburgh, PA) density gradient. Spleen and lymph nodes (LN) were dissociated mechanically. Splenocytes and blood were treated with ACK lysis buffer to lyse red blood cells.
The following antibodies were used for flow cytometry: anti-KLRG1 (2F1), anti-Eomes (Dan11ma), anti-T-bet (4B10), anti-CD44 (IM7), anti-CD122 (TM-b1), anti-CD27 (LG.7F9), anti-CD69 (H1.2F3) (all from eBioscience, San Diego, CA), anti-CD8α (53-6.7, eBioscience, Biolegend, San Diego, CA), anti-CD103 (M290), anti-CD25 (PC61), anti-Bcl-2 (Bcl-2/100) and anti-CD127 (SB/199) (BD Biosciences, San Jose, CA). Cell viability was determined using Ghost Dye^TM Red 780 (Tonbo Biosciences, San Diego, CA). K^b-SIINFEKL-specific CD8 T cells were identified using H-2K^b tetramers made in house containing the SIINFEKL peptide (New England Peptide, Gardener, MA). The BD Biosciences intracellular kit for cytokine staining and the eBioscience FoxP3 kit for transcription factor staining were used in accordance with manufacturer’s directions. Peptide stimulation was performed as previously described (30 (link)). Briefly, splenocytes were plated in RPMI 1640 containing 10% FBS, 1× NEAA, 2mM L-glutamine, 1mM sodium pyruvate, 1× penicillin/streptomycin and 0.05mM β-mercaptoethanol and incubated with 1ug/mL SIINFEKL peptide and 1ug/mL GolgiPlug (BD Biosciences, San Jose, CA) for four hours at 37°C. Cells were washed and stained with fixable LIVE/DEAD aqua dead cell stain (Life Technologies, San Diego, CA) before surface and intracellular staining. Samples were acquired on an LSRII flow cytometer (BD Biosciences, San Diego, CA).

Thompson E.A., Beura L.K., Nelson C.E., Anderson K.G, & Vezys V. (2016). Shortened intervals during heterologous boosting preserve memory CD8 T cell function but compromise longevity. Journal of immunology (Baltimore, Md. : 1950), 196(7), 3054-3063.

Publication 2016

2-Mercaptoethanol alpha HML-1 Antibodies BCL2 protein, human BLOOD Buffers CD8-Positive T-Lymphocytes CD44 protein, human Cells Cell Survival Collagenase, Clostridium histolyticum Cytokine Digestion Dithioerythritol Enzymes Erythrocytes Female Reproductive System Flow Cytometry Glutamine Hemoglobin, Sickle HEPES IL2RA protein, human IL2RB protein, human Intestines, Small Intraepithelial Lymphocytes isolation KB Cells KLRG1 protein, human Liver Lung Lymphocyte Magnesium Chloride Matrix Metalloproteinase 2 Mus Nodes, Lymph OVA-8 Penicillins Peptides Percoll Peyer Patches Protoplasm Pyruvate Red Cell Ghost Salivary Glands Sodium Spleen Stains Streptomycin Tetrameres Thomsen-Friedenreich antibodies Tissues Transcription Factor

Purification and Labeling of PBP

Cited 6 times

All experiments were performed in HEPES polymix buffer (pH 7.5) containing 5 mM NH₄Cl, 5 mM Mg(OAc)₂, 100 mM KCl, 0.5 mM CaCl₂, 8 mM putrescine, 1 mM spermidine, 5 mM HEPES and 1 mM dithioerythritol (DTE) at 37 °C with a free Mg²⁺ concentration of around 1.5 mM. MRE600 70S ribosomes were purified according to the published methods33 (link)41 (link). Nucleotide triphosphates were from GE-Healthcare. Plasmid construct for phosphate binding protein (PBP) was a kind gift from Prof. Martin Webb, London. The purification and 7-Diethylamino-3-((((2-Maleimidyl) ethyl)amino) carbonyl)coumarin (MDCC) labelling of PBP was done according to the published protocol32 (link).

Kiran Koripella R., Holm M., Dourado D., Mandava C.S., Flores S, & Sanyal S. (2015). A conserved histidine in switch-II of EF-G moderates release of inorganic phosphate. Scientific Reports, 5, 12970.

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Publication 2015

Buffers coumarin Dithioerythritol HEPES Nucleotides Phosphate-Binding Proteins Plasmids Putrescine Ribosomes Spermidine triphosphate

Most recents protocols related to «Dithioerythritol»

Quantification of Pteridine Metabolites

BH₄ and oxidized biopterins (BH₂ and biopterin) were determined by high-performance liquid chromatography (HPLC) followed by electrochemical and fluorescence detection, respectively, following an established protocol (32 (link)). Briefly, frozen heart samples were homogenized in ice-cold resuspension buffer, consisting of (in mmol · L⁻¹ ) 50 phosphate-buffered saline, 1 dithioerythriol, and 1 EDTA at pH 7.4. After centrifugation at 13,200 rpm for 10 min at 4°C, the supernatant was removed, and ice-cold acid precipitation buffer, consisting of (in mmol · L⁻¹) 1 phosphoric acid, 2 trichloroacetic acid, and 1 dithioerythritol, was added. Samples were vigorously mixed and then centrifuged for 15 min at 13,000 rpm and 4°C. Samples were injected into an isocratic HPLC system and quantified using sequential electrochemical (Coulochem III, ESA, Inc.) and fluorescence (Jasco) detection. HPLC separation was performed using a 250-mm ACE C-18 column (Hichrom) and a mobile phase comprised of 50 mM sodium acetate, 5 mM citric acid, 48 µΜ EDTA, and 160 µΜ dithioerythritol (pH 5.2) (all ultrapure electrochemical HPLC grade) at a flow rate of 1.3 mL/min. Background currents of +500 μA and −50 μA were used for the detection of BH₄ on electrochemical cells E1 and E2, respectively. 7,8-BH₂ and biopterin were measured using a Jasco FP2020 fluorescence detector set at 510-nm excitation and 595-nm emission. Quantification of BH₄, BH₂, and B was done by comparison with authentic external standards and normalized to sample protein content.

Chuaiphichai S., Chu S.M., Carnicer R., Kelly M., Bendall J.K., Simon J.N., Douglas G., Crabtree M.J., Casadei B, & Channon K.M. (2023). Endothelial cell-specific roles for tetrahydrobiopterin in myocardial function, cardiac hypertrophy, and response to myocardial ischemia-reperfusion injury. American Journal of Physiology - Heart and Circulatory Physiology, 324(4), H430-H442.

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Publication 2023

Acids Biopterin Buffers Cells Centrifugation Citric Acid Cold Temperature Dithioerythritol Edetic Acid Fluorescence Freezing Heart High-Performance Liquid Chromatographies Phosphates Phosphoric Acids Proteins Saline Solution Sodium Acetate Trichloroacetic Acid

Anaerobic 2-Oxoglutarate Dehydrogenase Assay

The E. coli strains were incubated in M9 medium supplied with 2 mM MgSO₄, 0.1 mM CaCl₂, 10 mM sodium nitrate, 0.01 mM NiCl₂, 0.01 mM FeCl₂, 50 μg/mL thiamine, and 20 μg/mL chloramphenicol under anaerobic conditions. To obtain anaerobic conditions, H₂ and CO₂ were used to purge the headspace of a bottle sealed with rubber. Approximately 4 × 10⁹ bacteria cells were collected by centrifugation (10,000× g, at 4 °C) from 750 mL medium and sonicated in Tris buffer (100 mM Tris-HCl at pH 8.4, 3 mM dithioerythritol) on ice in an anaerobic chamber (Coy Laboratory Products, Inc., Grass Lake, MI, USA) filled with 9% H₂, 15% CO₂, and 76% N₂ gas. The crude extracted proteins were collected from the supernatant by centrifugation (10,000× g, at 4 °C). The 2-oxoglutarate:ferredoxin oxidoreductase activity assays were performed using the method described in a previous report with modifications [15 (link)] in an anaerobic chamber (Coy Laboratory Products, Inc., Grass Lake, MI, USA). The activity of 2-oxoglutarate:ferredoxin oxidoreductase was determined by the reduction in succinyl-CoA (reduced methyl viologen:succinyl-CoA oxidoreductase). The assay was performed in a 1 mL volume containing 100 mM Tris-HCl at pH 8.4, 2 mM MgCl₂, 4 mM methyl viologen, and 1 mM succinyl-CoA. Dithionite was added from 1 M stock solutions until the methyl viologen-containing assay solutions presented a faint blue color. The optical density changes were measured at 578 nm (methyl viologen, ε₅₇₈ = 9.8 × 10³ M^–1 cm^–1) after addition of the succinyl-CoA solutions. The optical densities were measured with a GeneQuant 1300 (GE Healthcare, Little Chalfont, Buckinghamshire, UK) in the anaerobic chamber at 35 °C. The result is displayed in Table 2.

Cheng Y.C., Huang W.H., Lo S.C., Huang E., Chiang E.P., Huang C.C, & Yang Y.T. (2023). Conversion of Escherichia coli into Mixotrophic CO2 Assimilation with Malate and Hydrogen Based on Recombinant Expression of 2-Oxoglutarate:Ferredoxin Oxidoreductase Using Adaptive Laboratory Evolution. Microorganisms, 11(2), 253.

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Publication 2023

alpha-Ketoglutarate Bacteria Biological Assay Cells Centrifugation Chloramphenicol Dithioerythritol Dithionite Escherichia coli Ferredoxin Magnesium Chloride Oxidoreductase Paraquat Poaceae Proteins Rubber sodium nitrate Strains succinyl-coenzyme A Sulfate, Magnesium Syncope Thiamine Tromethamine Vision

Isolation of intestinal and splenic lymphocytes

To isolate lymphocytes from the spleen and MLN, tissues were mashed through 70-µm cell strainers. Small intestine LP lymphocytes and IEL were isolated as previously described (Qiu and Sheridan, 2018 (link); Sheridan and Lefrançois, 2012 (link)). Briefly, small intestines were cut into 1-inch long pieces after removal of Peyer’s patches and luminal content. Intestinal tissues were treated twice with 1 mM dithioerythritol (Sigma-Aldrich) solution in a shaker at 220 rpm and 37°C for 20 min. Supernatants were collected, combined, and subjected to 44%/67% Percoll (GE Healthcare) gradient for the isolation of IEL. The remaining intestine tissues were treated twice with 1.3 mM ethylenediaminetetraacetic acid (Invitrogen) solution in a shaker at 220 rpm and 37°C for 30 min to remove intestinal epithelial cells, followed by digestion with 100 U/ml of collagenase (Invitrogen) in a shaker at 300 rpm and 37°C for 45 min. Supernatants were collected after collagenase digestion and the undigested tissues were mashed through 70-µm cell strainers into the collected supernatant, which was then subjected to 44%/67% Percoll gradient for the isolation of LP lymphocytes.

Qiu Z., Khairallah C., Chu T.H., Imperato J.N., Lei X., Romanov G., Atakilit A., Puddington L, & Sheridan B.S. (2023). Retinoic acid signaling during priming licenses intestinal CD103+ CD8 TRM cell differentiation. The Journal of Experimental Medicine, 220(5), e20210923.

Publication 2023

Cells Collagenase Digestion Dithioerythritol Edetic Acid Epithelial Cells Intestines Intestines, Small isolation Lymphocyte Percoll Peyer Patches Phenobarbital Spleen Tissues

In Vitro Translation Assay Protocol

All in vitro translation experiments were conducted at 37 °C in HEPES–Polymix buffer (pH 7.5) (5 mM HEPES (pH 7.5), 95 mM KCl, 5 mM NH₄Cl, 5 mM Mg(OAc)₂, 8 mM putrescine, 0.5 mM CaCl₂, 1 mM spermidine and 1 mM 1,4-dithioerythritol) with additional energy regeneration components including 10 mM phosphoenolpyruvate (PEP), 50 μg/ml pyruvate kinase (PK), 2 μg/ml myokinase (MK), and 1 mM of ATP and GTP (unless otherwise specified). E. coli MRE600 cells were used to prepare tight-coupled 70S ribosomes following standard laboratory protocol. His-tagged clones of the translation factors (IF1, IF2, IF3, EF-Tu, EF-Ts, EF-G, RF1, RF2, RF3, and RRF) and Phenylalanine tRNA synthetase were overexpressed in E. coli BL21 (DE3) cells and purified using nickel-affinity chromatography (HiTrap; GE Healthcare). f[³H]Met-tRNA^fMet and tRNA^Phe were prepared as described^{17 (link)}. BODIPY^TM (BOP)•Met-tRNA^fMet was prepared as described earlier^{38 (link)}. In vitro transcribed XR7-mRNAs with strong Shine-Dalgarno sequence (AAGGAGG) and a small ORF AUGUUCUUCUAA (Met-Phe-Phe-stop), AUGCUCUUCUAA (Met-Leu-Phe-stop), AUGUUCUUCUUCUAA (Met-Phe-Phe-Phe-stop), and AUGUAA (Met-stop) were prepared according to Holm et al.^{35 (link)} Concentrations of the ribosomes, translation factors, tRNAs, and mRNAs were measured spectrophotometrically. THB (Thermorubin A) was purchased from AdipoGen Life Sciences and was dissolved in Dimethyl sulfoxide (DMSO) solution and stored at −20 °C. [³H] Met and [³H] GTP were from Perkin Elmer and all other chemicals were from either Merck or Sigma-Aldrich.

Parajuli N.P., Emmerich A., Mandava C.S., Pavlov M.Y, & Sanyal S. (2023). Antibiotic thermorubin tethers ribosomal subunits and impedes A-site interactions to perturb protein synthesis in bacteria. Nature Communications, 14, 918.

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Publication 2023

Buffers Cells Chromatography, Affinity Clone Cells Dithioerythritol elongation factor Ts Escherichia coli HEPES Kinase, Adenylate leucyl-phenylalanine Nickel Peptide Elongation Factor Tu Phenylalanine-Specific tRNA Phenylalanine-tRNA Ligase phenylalanyl-phenylalanyl-phenylalanine phenylalanylphenylalanine Phosphoenolpyruvate Putrescine Pyruvate Kinase Regeneration Ribosomes RNA, Messenger Spermidine Sulfoxide, Dimethyl thermorubin Transfer RNA

Subcellular Cr Fractionation in Leaf and Root

The subcellular fractionation of Cr in leaf and root tissues was quantified employing the procedure of Sheng et al. [108 (link)]. Briefly, fresh leaf and root material (0.5 g) was extracted in 10 mL of extraction buffer (1.0 mM DL-dithioerythritol, 0.25 mM sucrose, 5 mM AsA, and 50 mM Tris-HCl). The extract was filtered by using a nylon fabric with a mesh size of 100 mm and the filtrate was labelled as “cell wall fraction” (CWF) and subjected to centrifugation (15,000 rpm) for 45 min. The aliquot solution and resultant pellet were labelled as “soluble fraction” (SF) and “organelle fraction” (OF), respectively. These procedures were carried out at 4 °C. Both CWF and OF were transferred to an Erlenmeyer flask (100 mL) filled with deionized water, dried, and digested with HNO₃ (5 mL) [109 (link)]. Thereafter, Cr concentrations were determined with an ICP-OES (Perkin Elmer Optima 5300 DV).

Kaya C., Ugurlar F., Ashraf M., Alyemeni M.N., Moustakas M, & Ahmad P. (2023). 5-Aminolevulinic Acid Induces Chromium [Cr(VI)] Tolerance in Tomatoes by Alleviating Oxidative Damage and Protecting Photosystem II: A Mechanistic Approach. Plants, 12(3), 502.

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Publication 2023

Buffers Cell Wall Centrifugation Dithioerythritol Mesalamine Nylons Organelles Plant Leaves Plant Roots Radiotherapy Dose Fractionations Sucrose Tissues Tromethamine

Top products related to «Dithioerythritol»

Dithioerythritol by Merck Group

Sourced in United States, Germany

Dithioerythritol is a reducing agent commonly used in biochemical and molecular biology applications. It acts as a thiol-protecting agent, preventing the oxidation of sulfhydryl groups in proteins and other biomolecules.

Dithioerythritol dte by Merck Group

Sourced in United States

Dithioerythritol (DTE) is a reducing agent used in biochemical and molecular biology applications. It functions by maintaining a reducing environment, which is essential for the preservation and stability of various biomolecules such as proteins and nucleic acids.

Papain by Worthington

Sourced in United States, Germany, Japan, Austria

Papain is a proteolytic enzyme derived from the fruit of the papaya plant. It is a white to off-white powder with a neutral pH. Papain functions as a catalyst in the breakdown of proteins.

Collagenase type 2 by Worthington

Sourced in United States, United Kingdom, Jersey, Germany, Japan, Switzerland, Canada, Australia, France

Collagenase type II is an enzyme used in cell and tissue culture applications. It is responsible for the breakdown of collagen, a structural protein found in the extracellular matrix. This enzyme is commonly used to facilitate the dissociation of cells from tissues during cell isolation and harvesting procedures.

Trypsin by Promega

Sourced in United States, Germany, United Kingdom, China, Japan, France, Switzerland, Sweden, Italy, Netherlands, Spain, Canada, Brazil, Australia, Macao

Trypsin is a serine protease enzyme that is commonly used in cell culture and molecular biology applications. It functions by cleaving peptide bonds at the carboxyl side of arginine and lysine residues, which facilitates the dissociation of adherent cells from cell culture surfaces and the digestion of proteins.

Iodoacetamide by Merck Group

Sourced in United States, Germany, United Kingdom, Sao Tome and Principe, Italy, France, Macao, China, Canada, Australia, Switzerland, Spain

Iodoacetamide is a chemical compound commonly used in biochemistry and molecular biology laboratories. It is a reactive compound that selectively modifies cysteine residues in proteins, thereby allowing for the study of protein structure and function. Iodoacetamide is often used in sample preparation procedures for mass spectrometry and other analytical techniques.

C18 microspin column by Harvard Apparatus

Sourced in United States

The C18 microspin column is a laboratory equipment used for sample preparation and purification. It contains a C18 silica-based stationary phase that allows for the separation and concentration of analytes from complex matrices. The core function of this column is to facilitate the extraction and cleanup of target compounds prior to further analysis.

Formic acid by Merck Group

Sourced in Germany, United States, Italy, United Kingdom, France, Spain, China, Poland, India, Switzerland, Sao Tome and Principe, Belgium, Australia, Canada, Ireland, Macao, Hungary, Czechia, Netherlands, Portugal, Brazil, Singapore, Austria, Mexico, Chile, Sweden, Bulgaria, Denmark, Malaysia, Norway, New Zealand, Japan, Romania, Finland, Indonesia

Formic acid is a colorless, pungent-smelling liquid chemical compound. It is the simplest carboxylic acid, with the chemical formula HCOOH. Formic acid is widely used in various industrial and laboratory applications.

Porcine trypsin by Promega

Sourced in United States, Germany

Porcine trypsin is a proteolytic enzyme derived from the pancreas of pigs. It is commonly used in cell culture applications for the dissociation and disaggregation of adherent cells.

Dithioerythritol by Avantor

Sourced in Germany

Dithioerythritol is a reducing agent commonly used in biochemical applications. It functions by maintaining a reducing environment to prevent oxidation of sensitive molecules.

What are some common applications of Dithioerythritol?

How does the unique chemical structure of Dithioerythritol contribute to its functionality?

Are there different variations or types of Dithioerythritol available?

How can PubCompare.ai help optimize the use of Dithioerythritol in research?

PubCompare.ai's AI-driven platfrom allows researchers to more efficiently screen the scientific literature for protocols involving Dithioerythritol. The platform's analysis can help identify the most effective protocols and highlight key differences in protocol effectiveness, enabling researchers to choose the best option for their specific research goals and ensure reproducibility and accuracy. This can save time and unlock new insights in Dithioerythritol-related research.

More about "Dithioerythritol"

Dithioerythritol (DTE) is a synthetic organic compound with the chemical formula C4H8O2S2.
It is a reducing agent commonly used in biochemical and molecular biology applications, such as protein purification and enzyme assays.
Dithioerythritol has a unique dithiol structure that allows it to maintain reducing conditions and prevent oxidation of sensitive biomolecules.
Researchers can leverage PubCompare.ai's AI-driven platform to easily locate and compare dithioerythritol protocols from scientific literature, preprints, and patents, optimizing their research processes and unlocking new insights.
This versatile compound is often used in conjunction with other reagents like papain, collagenase type II, trypsin, iodoacetamide, C18 microspin columns, formic acid, and porcine trypsin to facilitate various biochemical procedures.
By exploring the power of PubCompare.ai's intuitive tools, researchers can streamline their dithioerythritol-based workflows, identify the best protocols and products, and unlock new discoveries in their fields of study.
PubCompare.ai's AI-driven platform provides a comprehensive solution for optimizing research processes and staying at the forefront of scientific advancements.