Log In Sign up
The largest database of trusted experimental protocols
> Chemicals & Drugs > Indicator > Reducing Agents

Reducing Agents

Reducing agents are substances that donate electrons and reduce other compounds.
They are commonly used in biochemical and chemical applications to create reducing environments, prevent oxidation, and facilitate reactions.
These agents include a diverse range of compounds such as thiols, ascorbic acid, and dithiothreitol.
Reducing agents play a crucial role in maintaining the stability and activity of biomolecules, controlling redox balance, and enabling the study of oxidation-sensitive processes.
Researchers utilize reducing agents to optimize experimental conditions, enhance reproducibility, and ensure the integrity of their findings.
Understanding the properties and applications of reducing agents is vital for designing robust research protocols and advancing scientific discoveries.

Most cited protocols related to «Reducing Agents»

1
Quantifying Peroxidase Activity of PMOs
Cited 33 times
The oxygen reactivity of PMOs was measured by a time resolved quantification of H2O2 formation in 96-well plates (total volume of 200 μL) using a Perkin Elmer EnSpire Multimode plate reader. All reactions were performed in 100 mM sodium phosphate buffer, pH 6.0 at 22°C. Based on preliminary studies ascorbate and CDH were used in concentrations of 30 μM and 0.3 μM (0.025 mg mL-1), respectively to prevent a limitation in the PMO reduction step. As electron donor for CDH 500 μM cellobiose was used. When ascorbate was used as reductant, it was added to a final concentration of 30 μM and enzyme assays were started by mixing 20 μL of the respective PMO with 180 μL of the ready-made assay solution containing 30 μM ascorbate, 50 μM Amplex Red and 7.14 U mL-1 peroxidase in 96-well plate wells. In reference experiments without PMO the background signal (H2O2 production by CDH) was measured and subtracted from the assays. When CDH was used as reductant, the PMO assays were started by mixing 20 μL of sample solution and 20 μL CDH solution with 160 μL of the reaction mix containing cellobiose, Amplex Red and peroxidase. Initial fluorescence scans of resorufin showed highest signal intensities and lowest interference with matrix compounds when using an excitation wavelength of 569 nm and an emission wavelength of 585 nm for the selected conditions. The stoichiometry of H2O2 conversion to resorufin formation is 1:1. By using a high concentration of Amplex Red (50 μM) the linearity of the detection reaction was ensured and the molar ratio of Amplex Red:H2O2 was always greater than 50:1
[22 (link)]. The H2O2 concentration in the assays was far below 1 μM, which leads to a linear concentration/activity response of horseradish peroxidase, which has a KM for H2O2 of 1.55 μM. The high final activity of horseradish peroxidase (7.14 U mL-1) assures a fast conversion of the formed H2O2 and prevents the final reaction to be rate limiting. Additionally, it prevents the accumulation of H2O2, which could have detrimental effects on enzyme stability in the assay. The stability of resorufin fluorescence under these conditions was tested by addition of varying concentrations of hydrogen peroxide (0.1 – 5 μM) to the assay. A stable signal that remained constant throughout the measured period of 45 minutes was observed and maximum signal intensity was reached already during the mixing period before starting the assay. A linear relation between fluorescence and H2O2 concentrations in the range of 0.1 – 2 μM H2O2 was observed and the slope (28450 counts μmol-1) was used for the calculation of an enzyme factor to convert the fluorimeters readout (counts min-1), into enzyme activity. PMO activity was defined as one μmol H2O2 generated per minute under the defined assay conditions.
Kittl R., Kracher D., Burgstaller D., Haltrich D, & Ludwig R. (2012). Production of four Neurospora crassa lytic polysaccharide monooxygenases in Pichia pastoris monitored by a fluorimetric assay. Biotechnology for Biofuels, 5, 79.
Publication 2012
Biological Assay Buffers Cellobiose Electrons enzyme activity Enzyme Assays Enzymes Enzyme Stability Fluorescence Horseradish Peroxidase Molar Oxygen Peroxidase Peroxide, Hydrogen Radionuclide Imaging Reducing Agents resorufin sodium phosphate Tissue Donors
2
Protein Fractionation and Analysis
Cited 29 times
For Figure 1, our procedure for obtaining cytoplasmic and nuclear protein fractions has been described previously (29 (link)). To obtain the insoluble protein fraction, the pellet that was not soluble in either the hypertonic or nuclear lysis buffers was resuspended in the same volume of cell lysis buffer as used to obtain soluble protein fractions (550 μl). The 10% Bis–Tris NuPage Gel (Invitrogen) was loaded with 20 μg of soluble protein and 40 μl of insoluble suspension, transferred via iBLOT (Invitrogen) to a nitrocellulose membrane, immunoblotted for HA and β-actin, and imaged as previously described (29 (link)) except that rat α-HA (3F10, Roche) diluted 1:1000 and goat anti-rat 800 diluted 1:15 000 were used to detect HA. For Figure 7, cells were harvested by scraping in PBS, washed once in PBS, and frozen. RIPA (Sigma) supplemented with PhosSTOP (Roche) and cOmplete ULTRA Tablets (Roche) inhibitors was added to each thawed cell pellet and cells were further lysed by freeze-thaw. Protein lysates were analyzed by Pierce BCA Protein Assay Kit (Thermo Scientific) and 25 μg protein was combined with NuPAGE sample buffer and reducing agent (Life Technologies), loaded onto 4–12% Bis–Tris gels (Life Technologies), and processed further as described above. Image Studio software (LiCOR) was used for quantification and further analysis was performed in Excel and GraphPad Prism.
For detection of Flag, the buffers and washes were Tris and milk-based as described elsewhere (30 (link)). The amount of unpurified protein sample loaded was 30 μl while the amount of purified protein sample loaded was 20 μl. The primary rabbit α-Flag antibody was diluted 1:1000 (Cell Signalling, Danvers, MA) and the secondary antibody was goat anti-rabbit HRP diluted 1:10 000 (Bio-Rad, Hercules, CA). The membrane was developed with SuperSignal West Pico Chemiluminescent Substrate (Thermo Pierce) and imaged on a ChemiDoc XRS+ (Bio-Rad). The membrane was stained with Ponceau S Staining Solution (Tocris Biosciences, Bristol, UK).
Woodard L.E., Downes L.M., Lee Y.C., Kaja A., Terefe E.S, & Wilson M.H. (2016). Temporal self-regulation of transposition through host-independent transposase rodlet formation. Nucleic Acids Research, 45(1), 353-366.
Publication 2016
Actins Biological Assay Bistris Buffers Cells Cytoplasm Freezing Gels Goat Immunoglobulins inhibitors Milk, Cow's Nitrocellulose Nuclear Protein ponceau S prisma Proteins Rabbits Radioimmunoprecipitation Assay Reducing Agents Tissue, Membrane Tromethamine
3
Midbrain Neuron Characterization Protocol
Cited 22 times
Midbrain slices were obtained from mice between postnatal ages 21 and 30. Mice were handled according to guidelines established by the Northwestern University Animal Care and Use Committee, the National Institutes of Health and the Society for Neuroscience. Midbrain slices were visualized using infrared-differential interference contrast (IR-DIC) video microscopy system (for patch clamp recording) and imaged with 2PLSM to measure calcium transients, mitochondrial membrane potential using TMRM dye, or mito-roGFP signal. SNc or VTA neurons were filled with Alexa594 and Fluo-4 and calcium transients were imaged as described previously 6 (link). Mitochondrial membrane potential was calculated using a Nernst equation describing the distribution of TMRM 11 (link). Transgenic mice were generated by conventional approaches with a roGFP2 construct containing the TH promoter and a matrix mitochondria-targeting sequence. Relative oxidation of mito-roGFP was determined from fluorescence measurements after fully reducing mitochondria with dithiothreitol and then fully oxidizing with aldrithiol. Since the calibrated signal becomes independent of absolute expression level of mito-roGFP, this strategy allows cell-to-cell comparisons. Results in the main body of the paper were derived from a single line of mice showing strong mito-roGFP expression. In the presence of a strong reducing agent as an estimate of roGFP concentration, we inferred that there was not a significant difference in the expression level between SNc and VTA neurons (Supplementary Figure 7). The oxidation state of mitochondria was also verified in a second line of mice having lower mito-roGFP expression levels (Supplementary Figure 7) and in cultured cells expressing mito-roGFP (Supplementary Figure 6). Single-cell reverse transcription-polymerase chain reaction (scRT-PCR) has been described previously 4. Relative gene expression of UCPs was performed by reverse transcriptase reaction followed by quantitative PCR analysis. Mn-SOD immunostaining used standard approaches. Sample “n” represents number of mice. Statistical analysis was performed with non-parametric test with threshold for significance less than 0.05.
Guzman J.N., Sanchez-Padilla J., Wokosin D., Kondapalli J., Ilijic E., Schumacker P.T, & Surmeier D.J. (2010). Oxidant stress evoked by pacemaking in dopaminergic neurons is attenuated by DJ-1. Nature, 468(7324), 696-700.
Publication 2010
Alexa594 Animals Calcium Cells Cultured Cells Dithiothreitol Fluo 4 Fluorescence Gene Expression Human Body Manganese Superoxide Dismutase Membrane Potential, Mitochondrial Mesencephalon Mice, Laboratory Mice, Transgenic Microscopy, Video Mitochondria Mitomycin Neurons Reducing Agents Reverse Transcriptase Polymerase Chain Reaction RNA-Directed DNA Polymerase Transients
4
Purification of Soluble GST Fusion Proteins
Cited 18 times
Soluble GST fusion proteins are purified easily using an immobilized glutathione Sepharose column. There are several options of immobilized glutathione chromatography media available to purify soluble GST fusion proteins from bacterial cell lysates (see Note 3). The protocol described below is an adaptation of the manufacturer’s recommendation using glutathione Sepharose 4B poured into a column and using a peristaltic pump to control flow rates. Protease inhibitors and reducing agents should be added to the buffers, as required, to minimize proteolysis of the fusion protein. An exception is that serine protease inhibitors must be removed from the glutathione buffer prior to enzymatic removal of the GST moiety, as they will inhibit enzyme activity (see Note 12). Save a small aliquot from each step of the purification for analysis by SDS-PAGE to monitor the location of the fusion protein throughout the purification (see Notes 13 and 14). A given column or batch of resin should be used exclusively with a single fusion protein to minimize potential cross contamination. As an alternative to column purification, a protocol describing batch purifications is described in Note 15. Batch purifications are quick and simple, but frequently the yield and purity of the protein obtained will be somewhat lower than that obtained through chromatographic separations. In order to minimize proteolysis, all steps of the protein purification should be carried out at 4 °C, unless otherwise noted.
Harper S, & Speicher D.W. (2011). Purification of proteins fused to glutathione S-tranferase. Methods in molecular biology (Clifton, N.J.), 681, 259-280.
Publication 2011
Acclimatization Buffers Cardiac Arrest Chromatography enzyme activity Enzymes Glutathione Peristalsis polyvalent mechanical bacterial lysate Protease Inhibitors Proteins Proteolysis Reducing Agents Resins, Plant SDS-PAGE Sepharose Sepharose 4B Serine Proteinase Inhibitors Staphylococcal Protein A
5
Western Blot Analysis of Protein Samples
Cited 10 times
Western blotting was conducted as previously described with modifications to protein preparation37 , 38 . Protein samples were combined with NuPAGE LDS Sample Buffer (4X) (Life Technologies, #NP0007) without any reducing agents and split into two aliquots for each sample. While one aliquot was for non-reducing analysis, beta-mercaptoethanol at 2% final concentration was added to the other aliquot for reducing analysis. All samples were incubated at 70 °C for 10 minutes before SDS-PAGE analysis. The primary antibodies and concentrations used for Western blotting were as follows: ACSL4 (1:2000, Santa Cruz Biotechnology, #sc-271800); HSPC300 (1:1000, Santa Cruz Biotechnology, #sc-390459); BAX (1:2000, #2772T), BAK (1:2000, #12105T), SLC3A2/4F2hc/CD98 (1:5000, #13180S), tubulin (1:5000, #2144S); filamin A (FLNA) (1:500, #4762S), filamin B (FLNB) (1:500, #12979S), myosin IIa (MYH9) (1:500, #3403S), talin-1 (TLN1) (1:500, # 4021S), SLC7A11 (1:1000, #12691S), CYFIP1 (1:1000, #44353S), WAVE-2 (1:1000, # 3659T), cleaved-caspase 3 (1:1000, #9661s), V5 (1:2000, #13202S; all from Cell Signaling Technology); glutathione antibody (1:1000, Abcam, #ab19534); actin (1:500, #MA5-11869, clone ACTN05 [C4]), NCKAP1 (1:1000, #PA5-30406; both from Thermo Fisher Scientific); drebrin (1:2000, #10260-1-AP), destrin (1:1000, #67657-1-Ig), Abi2 (1:1000, # 14890-1-AP), RPN1 (1:1000, #12894-1-AP; all from Proteintech); and vinculin (1:5000, Sigma-Aldrich, #V4505).
Atkin W.S., Hart A., Edwards R., Cook C.F., Wardle J., McIntyre P., Aubrey R., Baron C., Sutton S., Cuzick J., Senapati A, & Northover J.M. (2000). Single blind, randomised trial of efficacy and acceptability of oral Picolax versus self administered phosphate enema in bowel preparation for flexible sigmoidoscopy screening. BMJ : British Medical Journal, 320(7248), 1504-1509.
Publication 2023
2-Mercaptoethanol ABI2 protein, human Actins Antibodies Buffers Caspase 3 Clone Cells Destrin Filamin A Glutathione NCKAP1 protein, human Nonmuscle Myosin Type IIA Proteins Reducing Agents SDS-PAGE SLC3A2 protein, human Talin Tubulin Vinculin

Most recents protocols related to «Reducing Agents»

1
Quantifying Glycated CD59 Peptide
Not available on PMC !

Example 4

A sandwich-type ELISA assay is prepared that specifically quantifies GCD59 relative to the glycated CD59 (GCD59) peptide hybrid surrogate. Antibody H9 is used as a capture antibody to capture CD59 in samples tested. The detection antibody is developed using a peptide antigen containing a glucitollysine residue in the equivalent position of K41 in CD59. For this reason, these assays detect the reduced form of GCD59. These anti-glucitollysine GCD59 ELISA kit assays also include a sample preparation step that utilizes NaBH4 as the reducing agent for transformation of the glycated form of GCD59 into the reduced glycated form of GCD59. Kits include solutions of reducing agent in organic solvent to carry out this step.

Sandwich-type Amadori-modified GCD59 ELISA assays do not need sample preparation by NaBH4 reduction due to detection antibody specificity for the non-reduced Amadori-modified form of GCD59. Sample treatment with DTT may, however, improve antibody affinity.

US11866506B2. Anti-CD59 antibodies (2024-01-09). Mellitus, LLC [US]. Inventors: Michael Chorev [US], Jose A. Halperin [US].
Patent 2024
Antibody Affinity Antibody Specificity Antigens Biological Assay CD59 protein, human Enzyme-Linked Immunosorbent Assay glucitollysine Hybrids Immunoglobulins Peptides Reducing Agents Solvents Specimen Handling
2
Synthesis of VO2 Nanowires via Hydrothermal Method
Not available on PMC !

Example 1

VO2 nanowires were synthesized through a variation of the one-step hydrothermal method. Briefly, stoichiometric amounts of micron-sized V2O5 powder (Sigma-Aldrich, 98%) were placed in a polytetrafluoroethylene cup with deionized water (ρ=18.2 MΩ/cm, Barnstead Water Purification System) and a reducing agent (either 2-propanol or acetone). The cup was then sealed in an autoclave and heated at 210° C. for 18-72 hours. The synthesized powder was then vacuum filtered and washed with 2-propanol (Sample I), acetone (Sample A), and/or water. The powders were subsequently annealed at 550° C. under inert Ar atmosphere for several hours to obtain pure VO2 nanocrystals crystallized in the M1 phase upon cooling.

US11873383B2. Thermochromic fenestration films containing vanadium dioxide nanocrystals (2024-01-16). THE TEXAS A&M UNIVERSITY SYSTEM [US]. Inventors: Sarbajit Banerjee [US], Kate E. Pelcher [US], Nathan A. Fleer [US].
Patent 2024
Acetone Anabolism Atmosphere Polytetrafluoroethylene Powder Propanols Reducing Agents Vacuum vanadium pentoxide
3
Copper-Carbon Nanotube Composite Fabrication
Not available on PMC !

Example 1

5 mg of oxidized CNT (MWCNT, average size: 12 nm×10 μm) are dispersed in 60 ml of Tris-HCl 10 mM in water (pH 8.5). The solution is ultra-sonicated until good dispersion is observed (about 1 minute). Dopamine hydrochloride (DA) is then added to reach a concentration of 0.1 mg/ml and the dispersion is stirred during 24 hours (h) at room temperature.

Example 6

Pda-coated CNT obtained according to the 2nd coating protocol were dispersed in a 50%/50% (by volume) mixture of water and ethanol so as to arrive at a CNT concentration of 0.5 mg/ml. The dispersion was sprayed on a glass substrate heated at 70° C. The number of sprayed layers was 50.

Example 13

The pda-coated CNT layer of example 6 was used to test electroless deposition. The sample was immersed in an electroless deposition solution during the desired time. The electroless solution contained glyoxilic acid (0.2 M) as reducing agent, EDTA (Ethylenediaminetetraacetic acid, 0.03 M) and CuSO4 (0.03 M). The solution was heated to between 50 and 60° C. and the pH was adjusted to 12-12.5 using NaOH. The immersion of the sample in the electroless solution led to delamination of the CNT layer from the glass substrate, probably due to H2 bubbles trapped between the CNT layer and the substrate. Although relatively fragile, the CNT layer conserved its cohesion and kept floating in the solution. When the CNT layer was progressively filled by copper, it turned became a more and more stable Cu-CNT composite (FIG. 13). This fabrication path is interesting as it allows fabricating self-supported Cu-CNT composites.

It may be worthwhile noting that delamination is not a necessary process step but it may be used to produce very thin CNT tissues. The ampacity of the composite of example 13 was slightly increased compared to copper foil in same conditions (about 8·104 A/cm2). Although this was not tested, it is expected that using CNT coated with pda containing copper seeds would improve the copper filling with the electroless deposition technique.

Example 14

125 ml of tannic acid (0.01 mg/ml)+CuSO4·5H2O (0.6 mg/ml) were prepared in water. 20 mg of oxidized CNT were added to 50 ml of this solution. The dispersion was periodically ultra-sonicated while adding tannic acid CuSO4 solution until a volume of 125 ml was reached. The dispersion was then periodically ultra-sonicated during 20 minutes. 75 ml of Tris-HCl solution (10 mM) was added and periodical ultra-sonications were carried out during 30 minutes. The pH was adjusted to a value ranging from 11 to 12 and the coated CNT were filtrated.

Example 15

The metal-ion-seeded coated CNT of example 14 were dispersed in 40 ml ethanol/water mixture (50%/50% by volume) so as to arrive at a concentration of 0.5 mg/ml. The dispersion was then sprayed in several layers on a on a Si—TaN (10 nm)-Ta (15 nm)-Cu (150 nm) substrate using the Paasche VL series airbrush (distance from the substrate about 15 cm. The substrate temperature was 90° C. The resulting sprayed layer (FIG. 14) had a thickness of about 3.5 μm.

Example 16

The CNT layer of example 15 was subjected to electroplating in an aqueous 0.1 M CuSO4 solution (at room temperature). The pH was adjusted to 1 by addition of H2SO4. During the electroplating (potential: −0.2 V vs SCE, duration: 30 minutes) the solution was stirred. The resulting composite (FIGS. 15 and 16) had a thickness of about 5 μm.

While specific embodiments have been described herein in detail, those skilled in the art will appreciate that various modifications and alternatives to those details could be developed in light of the overall teachings of the disclosure. Accordingly, the particular arrangements disclosed are meant to be illustrative only and not limiting as to the scope of the invention, which is to be given the full breadth of the appended claims and any and all equivalents thereof.

US11873570B2. Metal-CNT composite, production method and materials therefor (2024-01-16). LUXEMBOURG INSTITUTE OF SCIENCE AND TECHNOLOGY (LIST) [LU]. Inventors: Antoine Duhain [LU], Marc Michel [LU], Guillaume Lamblin [BE], Damien Lenoble [BE].
Patent 2024
Acids Copper Edetic Acid Ethanol Figs Hydrochloride, Dopamine Light Metals Reducing Agents Submersion Tannins Teaching Tissues Tromethamine
4
Lyophilized Tetrofosmin Formulation: Optimized Composition
Not available on PMC !

Example 1

TABLE 1
Amount (% w/w)
Example Example Example Example
IngredientsABCD
Tetrofosmin13.00-15.0013.14-14.5314.7214.19
Disulfosalicylate
Stannous  0.37-0.5 0.37-0.46 0.44 0.43
Chloride
Dihydrate
Sodium D-12.00-16.0012.65-15.4714.9714.43
Gluconate
Sodium 50.00-62.0050.59-61.8454.8952.91
Bicarbonate
Gentisic Acid*15.00-17.0013.54-15.0014.9718.03
*Para-amino benzoic acid, Maleic acid, Anthranilic acid can also be used

Procedure:

Approximately 90% of the total volume of Water for Injection (WFI) was added to a preparation vessel. The WFI was deoxygenated. Tetrofosmin, reducing agent selected from stannous chloride dihydrate, transchelator selected from Sodium D-gluconate, radioprotectant selected from Gentisic acid, para-amino benzoic acid, maleic acid, anthranilic acid and combinations thereof and sodium hydrogen carbonate were dissolved. The solution obtained was deoxygenated and final volume and the bulk solution was deoxygenated. The solution was sterile filtered. The vials were partially stoppered and then lyophilized.

US11857647B2. Pharmaceutical composition comprising tetrofosmin and pharmaceutically acceptable salts thereof (2024-01-02). Jubilant Generics Limited [IN]. Inventors: Umamaheshwar M. Prasad [IN], Harmik Sohi [IN], Rahul Hasija [IN], Dinesh Kumar [IN], Kamal S. Mehta [IN], Raj Vijaya Kuniyil Kulangara [IN], Ashutosh Agarwal [IN], Dharam Vir [IN].
Patent 2024
Acids Amino Acids anthranilic acid Benzoic Acid Bicarbonate, Sodium Blood Vessel Dietary Fiber gentisic acid gluconate maleic acid Reducing Agents Sodium Sodium Chloride stannous chloride dihydrate Strains
5
Antibody Cysteine Mutant Conjugation
Not available on PMC !

Example 5

In addition to the previously described DTT reduction to uncap engineered single cysteine residues, TCEP reduction was also investigated. 27 different antibody cysteine mutants were investigated for conjugatability using THIOMAB approach with maleimide PEG (5 kDa) and TCEP. Both Coomassie and PEG staining of SDS-PAGE gels was used to detect PEGylation. However, Coomassie staining alone was used for conjugation ranking. Mutants were screened under non-reducing and reducing conditions (FIG. 15).

Mutants were ranked by different metrics, including conjugation efficiency (PAR) and selectivity (% mono-PEGylated, % un-PEGylated, and % multi-PEGylated heavy chain), as done with previous screening using DTT (FIG. 16 and FIG. 17).

Mutations K326C, T299C, A339C, K274C, G385C, Q386C, Y300C, K414C, S440C, S415C were identified as top 10 mutants with TCEP screening. Compared back to the original DTT screen, four mutants (A339C, K274C, S440C, G385C) are top 10 in conjugation using either TCEP or DTT uncapping.

The data shows that for the conjugation using TCEP, multi-PEGylation and PAR was reduced. The difference in conjugation efficiency between DTT and TCEP uncapping may be due to local hydrophobicity.

US11879004B2. Modified binding polypeptides for optimized drug conjugation (2024-01-23). GENZYME CORPORATION [US]. Inventors: Qun Zhou [US], Sunghae Park [US], Huawei Qiu [US], Marie-Priscille Brun [FR], Francis Duffieux [FR].
Patent 2024
Antibodies Cysteine Gels Genetic Selection Immunoglobulins maleimide Mutation Parent Reducing Agents SDS-PAGE tris(2-carboxyethyl)phosphine

Top products related to «Reducing Agents»

1
Nupage lds sample buffer by Thermo Fisher Scientific
Sourced in United States, United Kingdom, Germany, Denmark, France, Norway, Japan
The NuPAGE LDS sample buffer is a laboratory reagent used to prepare protein samples for electrophoresis analysis. It is designed to denature and solubilize proteins prior to separation by gel electrophoresis.
2
Nupage sample reducing agent by Thermo Fisher Scientific
Sourced in United States, United Kingdom
The NuPAGE Sample Reducing Agent is a laboratory reagent used to prepare protein samples for electrophoresis. It functions by reducing disulfide bonds in proteins, which helps to denature and unfold the protein structure. This facilitates more accurate separation and analysis of the individual protein components within the sample.
3
Reducing agent by Thermo Fisher Scientific
Sourced in United States, United Kingdom
Reducing agent is a chemical compound used in laboratory settings to facilitate chemical reactions by donating electrons and reducing the oxidation state of other substances. Its core function is to promote electron transfer and enable specific chemical transformations. No further extrapolation on intended use is provided.
4
Sample reducing agent by Thermo Fisher Scientific
Sourced in United States, Austria
The sample reducing agent is a chemical reagent used to prepare samples for various analytical techniques. It functions by reducing disulfide bonds in proteins, facilitating sample preparation and analysis.
5
Lds sample buffer by Thermo Fisher Scientific
Sourced in United States, United Kingdom, Germany
LDS sample buffer is a laboratory reagent used in the preparation of samples for protein analysis. It functions as a denaturing agent that helps unfold and solubilize proteins prior to electrophoresis or other analytical techniques. The buffer contains lithium dodecyl sulfate (LDS), a mild detergent, which disrupts non-covalent protein interactions and maintains the solubility of the denatured proteins.
6
Nupage reducing agent by Thermo Fisher Scientific
Sourced in United States, United Kingdom
NuPAGE reducing agent is a laboratory reagent used to break disulfide bonds in proteins, enabling their denaturation and separation during electrophoresis. It is a key component in the NuPAGE protein analysis system.
7
Bis tris gel by Thermo Fisher Scientific
Sourced in United States, United Kingdom, Germany, Japan, France, China, Italy, Canada, Australia
Bis-Tris gels are a type of polyacrylamide gel used for electrophoresis in biochemistry and molecular biology laboratories. They are designed to provide high-resolution separation of proteins under neutral or near-neutral pH conditions. The Bis-Tris buffer system maintains a stable pH throughout the electrophoresis run, which is important for the analysis of pH-sensitive proteins.
8
Pierce bca protein assay kit by Thermo Fisher Scientific
Sourced in United States, United Kingdom, Germany, China, Australia, Switzerland, France, Italy, Canada, Spain, Japan, Belgium, Sweden, Lithuania, Austria, Denmark, Poland, Ireland, Portugal, Finland, Czechia, Norway, Macao, India, Singapore
The Pierce BCA Protein Assay Kit is a colorimetric-based method for the quantification of total protein in a sample. It utilizes the bicinchoninic acid (BCA) reaction, where proteins reduce Cu2+ to Cu+ in an alkaline environment, and the resulting purple-colored reaction is measured spectrophotometrically.
9
Nupage 4 12 bis tris gel by Thermo Fisher Scientific
Sourced in United States, United Kingdom, Germany, France, Canada, Switzerland, Japan
The NuPAGE 4–12% Bis-Tris gel is a pre-cast polyacrylamide gel used for protein separation and analysis. It provides a consistent and reliable platform for electrophoretic separation of proteins in a Bis-Tris buffered system.
10
Nupage by Thermo Fisher Scientific
Sourced in United States, Germany, United Kingdom, France, Ireland, Denmark, Sweden
NuPAGE is a polyacrylamide gel electrophoresis (PAGE) system designed for the separation and analysis of proteins. It utilizes pre-cast, pre-formed gels that provide consistent, high-resolution protein separation. NuPAGE gels are available in various formats and pore sizes to accommodate a wide range of protein molecular weights.

More about "Reducing Agents"

Reducing agents are a diverse class of compounds that play a crucial role in maintaining the stability and activity of biomolecules, controlling redox balance, and enabling the study of oxidation-sensitive processes.
These substances, which include thiols, ascorbic acid, and dithiothreitol, donate electrons and reduce other compounds, creating reducing environments that prevent oxidation and facilitate reactions.
Researchers extensively utilize reducing agents in biochemical and chemical applications, such as in the NuPAGE LDS sample buffer and NuPAGE Sample Reducing Agent, to optimize experimental conditions, enhance reproducibility, and ensure the integrity of their findings.
Understanding the properties and applications of reducing agents is vital for designing robust research protocols and advancing scientific discoveries.
The NuPAGE 4-12% Bis-Tris gel, combined with the Pierce BCA Protein Assay Kit, represents a powerful tool for researchers studying oxidation-sensitive proteins and processes.
The NuPAGE reducing agent, a key component of the NuPAGE Sample Reducing Agent, helps maintain the stability and activity of these biomolecules during sample preparation and analysis.
By leveraging the insights gained from the MeSH term description and the capabilities of PubCompare.ai's AI-powered platform, researchers can streamline their research process, improve the quality of their results, and unlock new scientific breakthroughs.
Whether you're working with reducing agents, Bis-Tris gels, or other critical research tools, PubCompare.ai can help you identify the best protocols and products to suit your needs, ensuring the reproducibility and integrity of your findings.