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2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone

2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone is a organic compound with a quinone structure.
It has been studited for its potential biological and chemical applications.
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Most cited protocols related to «2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone»

The first assay measures succinyl-CoA ligase, SDH, glutamate dehydrogenase (GDH), fumarase, and malate dehydrogenase (MDH) (see below; Fig. 1). This assay is performed in 400 μl of medium A containing 50 mM KH2PO4 (pH 7.2) and 1 mg/ml BSA. The reduction of dichlorophenol indophenol (DCPIP) is measured using two wavelengths (600 nm and 750 nm) with various substrates and the electron acceptors decylubiquinone and phenazine methosulfate. The second assay measures α-ketoglutarate dehydrogenase (KDH), aconitase, and isocitrate dehydrogenase (IDG) activities. The same volume of the same medium is used, and pyridine nucleotide (NAD+/NADP+) reduction is measured with various substrates using wavelengths of 340 nm and 380 nm. In the third assay, citrate synthase is measured by monitoring dithionitrobenzene (DTNB; Ellman's reagent) reduction at wavelengths of 412 nm and 600 nm as previously described[19 (link)]. For this study, all measurements were carried out using a Cary 50 spectrophotometer (Varian Inc., Palo Alto, CA) equipped with an 18-cell holder maintained at 37°C. Protein was measured according to Bradford [31 (link)]. All chemicals were of the highest grade from Sigma Chemical Company (St Louis, MO).
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Publication 2010
2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone 2,6-Dichloroindophenol Aconitate Hydratase Biological Assay Cells Citrate (si)-Synthase Dithionitrobenzoic Acid Fumarate Hydratase Glutamate Dehydrogenase Isocitrate Dehydrogenase (NAD+) Ketoglutarate Dehydrogenase Complex Malate Dehydrogenase Methylphenazonium Methosulfate NADP Nucleotides Oxidants Proteins Pyridines Succinate-CoA Ligases
All assays were carried out in 10 mM Tris–SO4 (pH 7.4 at 32 °C), 250 mM sucrose, 2 mM MgSO4, and 1 mM K2SO4 at 32 °C unless otherwise stated. Gramicidin (20 μg ml−1) was included to dissipate the proton motive force in SMPs. Standard concentrations were 5 mM succinate, 2 mM NADP+, 60 μg ml−1 FumC, and 300 μg ml−1 MaeB. The NADPH concentration was followed at 340 to 380 nm (ε = 4.81 mM−1 cm−1) using a Molecular Devices SpectraMax Plus 384plate reader. The reductions of DCPIP (100 μM, 600 nm, ε = 21 mM−1 cm−1, blue to colorless) [14] (link) and INT (100 μM, 500 nm, ε = 19 mM−1 cm−1, colorless to red) [13] (link) were measured in the presence and absence of 100 μM decylubiquinone, 5 mM succinate, or 100 μM NADH. When required, ubiquinol oxidation by the respiratory chain was inhibited by 400 μM NaCN, and atpenin A5 (Santa Cruz Biotechnology, Santa Cruz, CA, USA) was used to inhibit complex II and added from a concentrated stocksolution in dimethyl sulfoxide (DMSO). O2 consumption by SMPs was measured using a Clark electrode in a stirred 1 ml Perspex cell held at 32 °C (Rank Brothers, Cambridge, UK).
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Publication 2013
2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone A-A-1 antibiotic ARID1A protein, human atpenin A5 Biological Assay Brothers Cardiac Arrest Cells Gramicidin Medical Devices NADH NADP Perspex Proton-Motive Force Respiratory Chain SDHD protein, human Succinate Sucrose Sulfate, Magnesium Sulfoxide, Dimethyl Tromethamine ubiquinol
Mitochondria from each brain region was isolated by differential centrifugation and purified through Percoll gradient to obtain non-synaptosomal mitochondria. “Non-synaptosomal mitochondria” includes the mitochondrial fraction minimally contaminated with synaptosomes, i.e., vesicles that arise from nerve terminals during tissue processing which rapidly reseal capturing other non-mitochondrial components [120] (link). Individual activities of each Complex were tested after lysing the organelles in 20 mM Hepes, pH 7.4 supplemented with proteolytic and phosphatase inhibitors (Sigma, cat # P2714 and P8849). NADH-decylubiquinone oxidoreductase (NQR), NADH-ferricyanide reductase (NFR), Succinate cytochrome c reductase (SCCR), Cytochrome c oxidase (CCO), ATPase, and citrate synthase activities were evaluated as described before in detail [32] (link).
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Publication 2012
2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone Adenosine Triphosphatases Brain Centrifugation Citrate (si)-Synthase HEPES inhibitors Mitochondria NADH NADH ferricyanide reductase Nerve Endings Organelles Oxidase, Cytochrome-c Oxidoreductase Percoll Phosphoric Monoester Hydrolases Proteolysis Succinate Cytochrome c Oxidoreductase Synaptosomes Tissues
Membrane vesicles were prepared from cultures of all mutants and wild type grown
in rich media at 30°C. Cultures were shaken at ∼230 rpm and harvested at
A600 = 1.4. The cells were harvested, as
previously described [32] (link), [45] (link). For proton translocation assays membranes underwent
a third centrifugation, 1 hour at 355,000×g. The membranes were tested for
deamino-NADH driven proton translocation by measuring the fluorescence quenching
of ACMA over the course of several minutes, using excitation and emission
wavelengths of 410 and 490 nm respectively. Deamino-NADH oxidase activity assays
and proton translocation assays were performed after the second centrifugation
in 50 mM MOPS, 10 mM MgCl2, pH 7.3 at room temperature, using 150
µg/ml membrane protein. Deamino-NADH oxidase activity was assayed using
oxygen as a terminal electron acceptor. The oxidase assays were started with
0.25 mM deamino-NADH (extinction coefficient 6.22 mM−1cm−1) and the absorbance monitored at 340 nm for 2 minutes.
Decylubiquinone was added from an ethanol stock to the reaction cuvette
containing membranes, and the samples were incubated for several minutes at room
temperature before addition of deamino-NADH. Complex I inhibitor capsaicin was
added at 0.3 mM from a 100 mM ethanol stock. The uncoupler FCCP was added to a
final concentration of 1 µM from a 1 mM ethanol stock. For proton
translocation assays, ACMA was added to 1 µM, while other concentrations
were the same as for oxidase assays. Ferricyanide reductase assays were
conducted at room temperature and the absorbance monitored at 410 nm for 2
minutes in buffer containing 10 mM potassium phosphate (pH 7.0), 1 mM EDTA, 1 mM
K3FeCN6, and 10 mM KCN [46] (link). 40–100 µg/ml of
membrane protein was used in each assay. Ferricyanide was used as the terminal
electron acceptor (extinction coefficient of 1.0 mM−1cm−1). The assays were started with 0.15 mM
deamino-NADH.
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Publication 2011
2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone Biological Assay Buffers Capsaicin Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone Cells Centrifugation Edetic Acid Ethanol Extinction, Psychological ferricyanide ferricyanide reductase Fluorescence Magnesium Chloride Membrane Proteins morpholinopropane sulfonic acid NADH NADH Dehydrogenase Complex 1 NADH oxidase nicotinamide-hypoxanthine dinucleotide Oxidants Oxidases potassium phosphate Proteins Protons Tissue, Membrane Translocation, Chromosomal
For measures of mitochondrial OXPHOS and citrate synthase activity, density-controlled male and female flies were aged separately for 15 days on standard media. Flies were gently homogenized in 1 mL chilled isolation buffer (225 mM mannitol, 75 mM sucrose, 10 mM MOPS, 1 mM EGTA, 0.5% fatty acid-free BSA, pH 7.2) using a glass-teflon dounce homogenizer. The extracts were centrifuged at 300 g for 5 minutes at 4°C. The supernatant was then centrifuged at 6,000 g for 10 minutes at 4°C to obtain a mitochondrial pellet. The pellet was resuspended in 100 µL of respiration buffer (225 mM mannitol, 75 mM sucrose, 10 mM KCl, 10 mM Tris-HCl, 5 mM KH2PO4, pH 7.2), aliquoted, and frozen at −80°C for enzyme activity assays. Protein was quantified in each mitochondrial sample using the BCA Protein Assay (Thermo Scientific, Rockford, IL, USA). We used these measures of protein abundance to standardize the amount of protein added to each reaction, and we optimized this amount separately for each enzyme assay. We assayed activity from six to eight biological replicates per sex for each genotype across either one or two blocks, with the activity of each biological replicate estimated from three technical replicate assays. We analyzed mitochondrial enzyme activities with analysis of variance models that included the fixed effects of mtDNA, nuclear genotype, sex, block and all interactions (Table S3).
The specific activity of complex I (NADH-ubiquinone reductase) was determined as the rotenone-sensitive rate, following the oxidation of NADH at 340 nm with the coenzyme Q analog decylubiquinone as the electron acceptor. The reaction mixture contained 35 mM NaH2PO4, 5 mM MgCl2, 2.5 mg/mL BSA, 2 mM KCN, 2 µg/mL antimycin A, 100 µM NADH, 100 µM decylubiquione and 15 µg mitochondrial protein, and was inhibited with 2 mM rotenone. The catalytic activity of complex II (succinate dehydrogenase) was monitored by the reduction of DCPIP at 600 nm. The reaction mixture contained 30 mM NaH2PO4, 100 µM EDTA, 2 mM KCN, 2 µg/mL antimycin A, 2 µg/mL rotenone, 750 µM BSA, 10 mM succinate, 100 µM DCPIP, 100 µM decylubiquinone and 15 µg mitochondrial protein, and was inhibited with 400 mM malonate. Complex III (cytochrome c reductase) activity was measured by monitoring the reduction of cytochrome c at 550 nm. The reaction mixture contained 35 mM NaH2PO4, 2.5 mg/mL BSA, 5 mM MgCl2, 2 mM KCN, 2 µg/mL rotenone, 50 µM cytochrome c, 25 µM decylubiquinol and 7 µg mitochondrial protein, and was inhibited with 5 µg/mL antimycin A. Potassium borohydride was used to reduce decylubiquione. Complex IV (cytochrome c oxidase) activity was measured by determining the rate of oxidation of reduced cytochrome c at 550 nm. The reaction mixture contained 5 mM MgCl2, 2 µg/mL Rotenone, 2 µg/mL Antimycin A, 1 mM DDM, 60 µM cytochrome c and 15 µg mitochondrial protein, and was inhibited with 4 mM KCN. Sodium dithionite was used to reduce cytochrome c. Equine heart cytochrome c was obtained from Sigma-Aldrich (C7752). To measure citrate synthase activity, the rate limiting reaction of citrate synthase was coupled to a chemical reaction in which DTNB reacts with CoA-SH and the absorbance of the product is measured at 412 nm. The reaction mixture contained 100 µM DTNB, 300 µM acetylCoA, 100 mM TrisHCl, 300 µM oxaloacetic acid and 6 µg mitochondrial protein.
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Publication 2013
2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone Antimycin A Biological Assay Biopharmaceuticals Buffers Cell Respiration Citrate (si)-Synthase CoASH Coenzyme A, Acetyl Coenzymes Cytochromes c Diptera Dithionitrobenzoic Acid DNA, Mitochondrial DNA Replication Edetic Acid Egtazic Acid Electron Transport Complex III enzyme activity Enzyme Assays Equus caballus Fatty Acids Females Freezing Genotype Heart isolation Magnesium Chloride Males malonate Mannitol Mitochondria Mitochondrial Proteins morpholinopropane sulfonic acid NADH NADH Cytochrome c Oxidoreductase NADH Dehydrogenase Complex 1 Oxaloacetic Acid Oxidants Oxidase, Cytochrome-c potassium borohydride Proteins Rotenone SDHD protein, human Sodium Dithionite Succinate Succinate Dehydrogenase Sucrose Teflon Tromethamine ubidecarenone

Most recents protocols related to «2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone»

Preparation of histidine-tagged recombinant P. oryzae DHODH (PoDHODH) and N-terminal truncated H. sapience DHODH (ΔN-HsDHODH) protein, that the N-terminal 1-28 amino acids truncated from full length HsDHODH takes a role of import and proper location and fixation of the enzyme in the inner mitochondrial membrane,9 (link)) is described in the supplementary material. The DHODH activity was measured using PoDHODH and ΔN-HsDHODH proteins following the previously described protocol.2 (link),8 (link),10 (link)) The oxidation of the substrate dihydroorotate with the quinone co-substrate was coupled to reduce the chromogen 2,6-dichloroindophenol (DCIP). One hundred microliters of reaction mixture containing 50-mM Tris-HCl (pH 8.0), 150-mM NaCl, 0.1% (w/v) TritonX-100, 200-μM DCIP, 2-mM dihydroorotate, 100-μM decylubiquinone (QD), approximately 10-µg/mL recombinant PoDHODH or ΔN-HsDHODH protein suspension, and various concentrations of test compounds dissolved in 1% DMSO (or no compound control) were incubated at 30°C for 20–30 min. After incubation, 10-µL 10% sodium dodecyl sulfate was added to each sample and mixed well to stop the reaction. Then, absorbance at 595-nm was measured. The inhibitory rate was calculated as (1-T/C), where C and T represent the decreased absorbance quantity at 595-nm with the control and test samples, respectively. The IC50 (half-inhibition concentration) values for the test compounds on PoDHODH and ΔN-HsDHODH were determined using a four-parameter logistic curve-fitting program (GraphPad Prism 6.00), in which two parameters were constrained (i.e., the top and bottom were fixed as 1 and 0).
Publication 2023
2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone Amino Acids azo rubin S dihydroorotate Dihydroorotate Dehydrogenase Enzymes Histidine Mitochondrial Membrane, Inner prisma Proteins Psychological Inhibition Quinones Sodium Chloride Sulfate, Sodium Dodecyl Sulfoxide, Dimethyl Tromethamine
All activity measurements were measured on a 96-well Spectramax 384 plate reader at 32°C. For NADH:decylubiquinone (dQ) oxidoreductase activities, NADH (200 µM final concentration) was used to initiate catalysis by complex I (0.2 µg mL–1) with 200 µM dQ, 0.15% (w/v) asolectin, and 0.15% (w/v) CHAPS in 20 mM Tris-HCl (pH 7.55). NADH oxidation was monitored at 340–380 nm (ε = 4.81 mM–1 cm–1), and was confirmed to be sensitive to rotenone and piericidin A. The cryo-EM sample had an activity of 7.3 ± 0.3 µmol min–1 mg–1 (mean ± SD; n = 4).
For evaluation of the active/deactive state ratio of Drosophila complex I using the N-ethylmaleimide (NEM) assay (Galkin et al., 2008 (link); Yin et al., 2021 (link)), 4 mg mL–1 mitochondria were incubated with 2 mM NEM or the equivalent volume of DMSO on ice for 20 min., before determining the NADH:O2 oxidoreductase activity. The mitochondria had been frozen for storage before measurement. To attempt to deactivate the complex, the mitochondria were incubated at 37°C for 30 min (equivalent to, or longer than, the treatments used to deactivate complex I in mammalian mitochondrial membranes [Agip et al., 2018 (link); Blaza et al., 2018 (link)]). NADH:O2 oxidoreductase activities were measured in 20 mM Tris-HCl (pH 7.55) using 10 µg mL–1 mitochondria and 10 µg mL–1 alamethicin, and initiated using 200 µM NADH. NADH oxidation was monitored as described above.
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Publication 2023
2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate Alamethicin asolectin Biological Assay Catalysis Drosophila Ethylmaleimide Freezing Mammals Mitochondria NADH NADH Dehydrogenase Complex 1 Oxidoreductase piericidin A Rotenone Sulfoxide, Dimethyl Tissue, Membrane Tromethamine
PfMQO enzyme was prepared using PfMQO-expressing recombinant Escherichia coli, as described by Hartuti et al. (2018) [11 (link)]. The principle of the PfMQO assay is shown in Figure 2a. An assay mix solution was prepared from 50 mM HEPES-KOH (pH 7.5), 1 mM KCN, 60 µM decylubiquinone, 120 µM DCIP (blue), and 3 µg of PfMQO-membrane fraction. Further, 193 µL of the assay mix was transferred to a 96-well microplate, and 2 µL of microbial extract was added. The reaction was started by the addition of 5 µL of 400 mM sodium-L-malate (Wako) and subsequently mixed using a plate mixer (800–1000 rpm) for 30 seconds. The absorbance of the mixture was recorded by a SpectraMax®® Paradigm®® multi-mode multiplate reader (Molecular Devices, California, USA). The inhibitory activity was calculated using a formula, as described in Figure 2b. The reaction mixture without the addition of the substrate and microbial extract was regarded as the positive control (PC) and negative control (NC), respectively.
The performance of the screening system was evaluated by calculating the statistical parameter, z’factor, with the following Equation [22 (link)]
zfactor=13SD of PC +3SD of NCmean of PC  mean of NC
where SD is the standard deviation; PC is the positive control; and NC is the negative control.
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Publication 2023
2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone Biological Assay Enzymes Escherichia coli Fibrinogen HEPES malate Medical Devices Neoplasm Metastasis Psychological Inhibition SAMHD1 protein, human Sodium Tissue, Membrane
An equal amount of isolated mitochondria were suspended in 0.05 M KP buffer containing 20 mM succinate, 300 µM sodium azide, 80 µM DCPIP, and BSA (1 mg/mL). The mitochondrial suspension was incubated at 370C for 10 min. Complex II activity was initiated with the addition of decyl ubiquinone (50 µM), and its activity was monitored in a spectrophotometer as a decrease in absorbance at 600 nM.
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Publication 2023
2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone Buffers Mitochondria SDHD protein, human Sodium Azide Succinate
The linearity range of CjMQO activity was evaluated using a dose-response curve following a method reported previously with several modifications (Hartuti et al., 2018 (link); Acharjee et al., 2021 (link)). The spectrophotometric assay was performed in triplicate at 37°C with a spectrophotometer (V760, Jasco Co., Tokyo, Japan) connected to an open bath circulator (Julabo ED, Julabo Labortechnik GmbH, Germany). The CjMQO concentrations ranged from 0.01 to 2 μg/mL in a 1 mL reaction mixture containing 50 mM HEPES (pH 7.0), 20 μM decylubiquinone (dUQ, Sigma-Aldrich Inc.), 1 mM potassium cyanide (KCN, Sigma-Aldrich Inc.) and 120 μM 2,6-dichlorophenolindophenol (DCIP, Sigma-Aldrich Inc.). The reaction was started by adding 10 mM sodium malate to the reaction mixture, and the reduction of DCIP was measured at 600 nm. The specific activity was calculated by using the extinction coefficient ( ε600 ) of DCIP of 21 mM-1 cm-1. The optimum temperature for the activity of purified CjMQO was determined in triplicates under different temperatures as indicated above at fixed concentration of 0.2 μg/mL of purified CjMQO.
The optimum pH was determined as described previously (Hartuti et al., 2018 (link); Acharjee et al., 2021 (link)) by measuring CjMQO activity at different pH values using 50 mM of HEPES-NaOH (pH 6.8–8.4), Tris-HCl (pH 6.9–9.0), sodium phosphate (NaPi, pH 5.8–8.0), potassium phosphate (KPi, pH 5.8–8.0), MOPS-NaOH (pH 6.5–8.9), and CHES-NaOH (pH 8.6–10.0) buffers at 37°C and 0.2 μg/mL of purified CjMQO with a multi-mode microplate reader (SpectraMax Paradigm, Molecular Devices, San Jose, CA, United States).
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Publication 2023
2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone 2,6-Dichloroindophenol 2-(N-cyclohexylamino)ethanesulfonic acid Bath Biological Assay Buffers Extinction, Psychological HEPES malate Medical Devices morpholinopropane sulfonic acid Potassium Cyanide potassium phosphate SAMHD1 protein, human Sodium sodium phosphate Spectrophotometry Tromethamine

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Decylubiquinone is a laboratory reagent used in the study of electron transport and oxidative phosphorylation processes in biological systems. It is a synthetic analogue of the naturally occurring coenzyme Q10 (ubiquinone) with a decyl side chain. Decylubiquinone serves as an electron acceptor and can be used to investigate the function and activity of various enzymes and complexes involved in cellular respiration.
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Antimycin A is a chemical compound that acts as a potent inhibitor of mitochondrial respiration. It functions by blocking the electron transport chain, specifically by interfering with the activity of the cytochrome bc1 complex. This disruption in the respiratory process leads to the inhibition of cellular respiration and energy production within cells.
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Rotenone is a naturally occurring insecticide and piscicide derived from the roots of certain tropical plants. It is commonly used as a research tool in laboratory settings to study cellular processes and mitochondrial function. Rotenone acts by inhibiting the electron transport chain in mitochondria, leading to the disruption of cellular respiration and energy production.
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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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Cytochrome c is a heme-containing protein found in the electron transport chain of mitochondria. It functions as an electron carrier, facilitating the transfer of electrons between Complexes III and IV during the process of oxidative phosphorylation. Cytochrome c plays a crucial role in cellular respiration and energy production.
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The Mitochondrial Complex I Activity Colorimetric Assay Kit is a laboratory tool designed to measure the activity of Complex I, also known as NADH:ubiquinone oxidoreductase, within the electron transport chain of mitochondria. The kit utilizes a colorimetric method to quantify the oxidation of NADH, providing a direct assessment of Complex I enzymatic function.
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The SpectraMax Plus 384 is a high-performance microplate reader that provides precise and reliable absorbance, fluorescence, and luminescence measurements. It features a 384-well microplate format, enabling efficient and high-throughput assays. The instrument offers a wide range of wavelengths, making it suitable for a variety of applications in life science research and drug discovery.
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Succinate is a laboratory equipment product that serves as a chemical compound. It functions as a dicarboxylic acid and is a key intermediate in the citric acid cycle, a central metabolic pathway in many organisms.
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The Synergy H1 is a multi-mode microplate reader designed for a variety of applications. It is capable of absorbance, fluorescence, and luminescence detection.
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Oligomycin is a laboratory product manufactured by Merck Group. It functions as an inhibitor of the mitochondrial F1F0-ATP synthase enzyme complex, which is responsible for the synthesis of adenosine triphosphate (ATP) in cells. Oligomycin is commonly used in research applications to study cellular bioenergetics and mitochondrial function.

More about "2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone"

2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone, also known as Decylubiquinone, is an organic compound with a quinone structure.
This versatile molecule has been studied extensively for its potential biological and chemical applications.
As a derivative of the ubiquinone (Coenzyme Q) family, Decylubiquinone plays a crucial role in mitochondrial electron transport and energy production.
It is closely related to Antimycin A and Rotenone, two other quinone-based compounds with important functions in biological systems.
Decylubiquinone has been investigated for its ability to modulate Cytochrome c and Mitochondrial Complex I Activity, key components of the cellular respiration process.
Researchers have utilized assays like the Mitochondrial Complex I Activity Colorimetric Assay Kit and instruments like the SpectraMax Plus 384 to study the effects of this compound on mitochondrial function.
Furthermore, Decylubiquinone has demonstrated potential applications in the fields of bioenergetics and pharmacology.
Its ability to interact with Succinate and other biomolecules has made it a subject of interest for scientists studying cellular metabolism and energy pathways.
To optimize research on Decylubiquinone, researchers can leverage platforms like PubCompare.ai to locate the most reliable and effective protocols from literature, preprints, and patents.
This can enhance reproducibility, save time, and ensure that your work is built on the strongest foundations.
By exploring the varied applications and properties of this fascinating quinone compound, researchers can unlock new insights and drive advancements in diverse areas of science and technology.
Whether your focus is on bioenergetics, pharmacology, or beyond, Decylubiquinone and its related compounds offer a wealth of opportunities for discovery and innovation.