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Coenzyme A

Coenzyme A is a critical cofactor involved in numerous metabolic processes, including energy production, fatty acid synthesis, and the citric acid cycle.
It consists of a pantothenic acid moiety linked to a β-mercaptoethylamine group and an adenosine 5'-diphospho group.
Coenzyme A plays a central role in the metabolism of carbohydrates, lipids, and amino acids, and its accurate quantification and study is essential for understanding cellular energetics and regulatory pathways.
Researchers can leverage PubCompare.ai, an AI-driven platform, to optimize their Coenzyme A reseach protocols for reproducibility and accuracy by easily locating and comparing methods from the literature, preprints, and patents to identifiy the best approcahes and products for their experiments.
The AI-powered comparisons on PubCompare.ai can help ensure Coenzyme A research is efficient and reliable.

Most cited protocols related to «Coenzyme A»

1
Cell-Free Protein Synthesis Protocol
The CFPS reactions were carried out in a 1.5 mL microtube in the incubator. The standard reaction mixture for CFPS consists of the following components in a final volume of 15 μL: 1.2 mM ATP; 0.85 mM each of GTP, UTP, and CTP; 34.0 μg mL−1 L-5-formyl-5, 6, 7, 8-tetrahydrofolic acid (folinic acid); 170.0 μg mL−1 of E. coli tRNA mixture; 130 mM potassium glutamate; 10 mM ammonium glutamate; 12 mM magnesium glutamate; 2 mM each of 20 amino acids; 10 μM of L-[14C(U)]-leucine (11.1 GBq mmol−1, PerkinElmer, Waltham, MA); 0.33 mM nicotinamide adenine dinucleotide (NAD); 0.27 mM coenzyme-A (CoA); 1.5 mM spermidine; 1 mM putrescine; 4 mM sodium oxalate; 33 mM phosphoenolpyruvate (PEP); 13.3 μg mL−1 plasmid; 100 μg mL−1 T7 RNA polymerase, and 27% v/v of cell extract. The CFPS reactions were carried out at 37°C for 4 hours.
Kwon Y.C, & Jewett M.C. (2015). High-throughput preparation methods of crude extract for robust cell-free protein synthesis. Scientific Reports, 5, 8663.
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Publication 2015
5,6,7,8-tetrahydrofolic acid Amino Acids Ammonium bacteriophage T7 RNA polymerase Cell Extracts CFP protocol Coenzyme A Coenzyme I Escherichia coli Glutamates Leucine Leucovorin Magnesium Phosphoenolpyruvate Plasmids Potassium Glutamate Putrescine Sodium Oxalate Spermidine Transfer RNA
2
Belimumab for Systemic Lupus Erythematosus
In this phase 3, multicenter, randomized, double-blind, placebo-controlled trial, patients with SLE on SOC therapy were assigned to receive placebo, or belimumab 1 or 10 mg/kg by intravenous (IV) infusion over 1 hour on days 0, 14, and 28, and every 28 days through week 72. While the initiation of an immunosuppressive (IS) drug was prohibited during the trial, the addition of a new antimalarial (AM) drug and dose increases of concomitant IS or AM drugs were permitted until week 16. After week 16, however, the maximum doses of IS or AM drugs could be no greater than the higher of the baseline or week-16 dose. For corticosteroids, any dose was permitted through week 24; thereafter through week 44, the dose had to be within 25% or 5 mg of baseline. Between weeks 44 and 52, no increase over the higher of the baseline or week-44 dose was permitted. From weeks 52 through 68, the dose had to be within 25% or 5 mg of baseline, and an increase over the higher of the baseline or week-68 dose was prohibited after week 68. Prednisone could be reduced at the discretion of the investigator. As in the companion phase 3 BLISS-52 trial, the addition of a new biologic agent at any time, an inhibitor of the renin-angiotensin system after 4 months, or a new 3-hydroxy-3-methylglutaryl-coenzyme A reductase inhibitor after 6 months was prohibited; other antihypertensive or lipid-lowering agents were allowed during the study (17 (link)). The Safety of Estrogens in Lupus Erythematosus National Assessment–SLE Disease Activity Index (SELENA-SLEDAI) (18 (link)), Physician’s Global Assessment (PGA) (18 (link)), British Isles Lupus Assessment Group (BILAG) (19 (link),20 (link)), and SLE Flare Index (SFI) (21 (link)) were evaluated every 4 weeks (except weeks 56 and 64), as were AEs, vital signs, concomitant medications, and laboratory and pregnancy tests.
Furie R., Petri M., Zamani O., Cervera R., Wallace D.J., Tegzová D., Sanchez-Guerrero J., Schwarting A., Merrill J.T., Chatham W.W., Stohl W., Ginzler E.M., Hough D.R., Zhong Z.J., Freimuth W, & van Vollenhoven R.F. (2011). A Phase 3, Randomized, Placebo-Controlled Study of Belimumab, a Monoclonal Antibody That Inhibits BLyS, in Patients With Systemic Lupus Erythematosus. Arthritis and rheumatism, 63(12), 3918-3930.
Publication 2011
Adrenal Cortex Hormones Angiotensins Antihypertensive Agents Antimalarials belimumab Biological Factors Coenzyme A Estrogens Hypolipidemic Agents Immunosuppressive Agents Intravenous Infusion Lupus Vulgaris Oxidoreductase Patients Pets Pharmaceutical Preparations Physicians Placebos Prednisone Pregnancy Tests Renin Inhibitors Safety Signs, Vital Therapeutics
3
Comprehensive HIV Cohort Analysis Protocol
We determined age, sex, and race/ethnicity using administrative data. Hypertension, diabetes mellitus,12 (link) dyslipidemia, renal disease, and anemia were measured using outpatient and clinical laboratory data collected closest to the baseline date. The HMG-CoA [(3-hydroxy-3-methylglutaryl)–coenzyme A] reductase-inhibitor use and ART were based on pharmacy data, and smoking and body mass index (BMI; calculated as weight in kilograms divided by height in meters squared) were measured from health factor data that are collected in a standardized form within the VA. Hypertension was categorized as no hypertension (blood pressure <140/90 mm Hg and no anti-hypertensive medication), controlled hypertension (<140/90 mm Hg with antihypertensive medication), and uncontrolled hypertension (2:140/90 mm Hg).13 (link) Our blood pressure measurement was the average of the 3 routine outpatient clinical measurements closest to the baseline date. Diabetes was diagnosed using a previously validated metric that considers glucose measurements, antidiabetic agent use, and/or at least 1 inpatient and/or 2 or more outpatient ICD-9 codes for this diagnosis.12 (link) The HMG-CoA reductase-inhibitor use was within 180 days of the baseline date. Current, past, and never smoking and BMI were assessed using documentation from the VA electronic medical record health factor data set, which contains information collected from clinical reminders that clinicians are required to complete for patients. Prior work14 (link) demonstrates the high agreement between health factor documentation and VACS-8 self-reported smoking survey data. Hepatitis C virus infection was defined as a positive hepatitis C virus antibody test result or at least 1 inpatient and/or 2 or more outpatient ICD-9 codes for this diagnosis.15 (link) History of cocaine and alcohol abuse or dependence was defined using ICD-9 codes.16 (link) We collected data on CD4 cell counts and HIV-1 RNA values from baseline through the last follow-up date. Baseline and recent ART was categorized by drug class and types of regimen within 180 days of the baseline enrollment date and the date closest to AMI, death, or last follow-up date, respectively. Regimen was defined as protease inhibitors plus nucleoside reverse-transcriptase inhibitors (NRTI), nonnucleoside reverse-transcriptase inhibitors (NNRTI) plus NRTI, other, and no ART use (ie, reference). Prior work7 (link) demonstrated in a nested sample that 96% of HIV-positive veterans obtain all their ART medications from the VA.
Freiberg M.S., Chang C.C., Kuller L.H., Skanderson M., Lowy E., Kraemer K.L., Butt A.A., Bidwell Goetz M., Leaf D., Oursler K.A., Rimland D., Rodriguez Barradas M., Brown S., Gibert C., McGinnis K., Crothers K., Sico J., Crane H., Warner A., Gottlieb S., Gottdiener J., Tracy R.P., Budoff M., Watson C., Armah K.A., Doebler D., Bryant K, & Justice A.C. (2013). HIV Infection and the Risk of Acute Myocardial Infarction. JAMA internal medicine, 173(8), 614-622.
Publication 2013
3-hydroxy-3-methylglutaryl-coenzyme A Abuse, Alcohol Anemia Antidiabetics Antihypertensive Agents Blood Pressure CD4+ Cell Counts Clinical Laboratory Services Cocaine Coenzyme A Determination, Blood Pressure Diabetes Mellitus Diagnosis Dyslipidemias Ethnicity Factor Va Glucose Hepatitis C Antibodies Hepatitis C virus High Blood Pressures HIV-1 HIV Seropositivity Hydroxymethylglutaryl-CoA Reductase Inhibitors Index, Body Mass Inpatient Kidney Diseases Nucleosides Outpatients Oxidoreductase Patients Pharmaceutical Preparations Protease Inhibitors Reverse Transcriptase Inhibitors Treatment Protocols Veterans
4
Optimizing Cellular Metabolism through Quadratic Programming
The set of metabolite concentrations ([met]) and reaction free energies (ΔG) associated with central carbon metabolism (CCM; see Supplementary Fig. 4) that best matched i) the directly observed concentrations for measured metabolites ([met]exp) and ii) the observed cellular ΔG for measured reactions (ΔGexp) were computed. An important consideration in this calculation is that literature values for ΔG°′ may themselves contain error. In addition, these ΔG°′ values are interrelated, such that ΔG°′ for any sequence of metabolic reactions must be given by the sum of the formation energies of the products minus the formation energies of the reactants. Accordingly, we set out to optimize both metabolite concentrations and formation energies so as to maximize consistency with prior estimates of ΔfG°′ based on the component contribution method (which itself incorporates prior literature data on ΔG°′) and our experimental observations of metabolite concentrations and cellular reaction free energies. To this end, a quadratic programming problem was formulated with independent variables ln[met] and ΔfG°′, with the optimization objective of minimizing the departure from the expected ΔfG°′ and measured ln[met] and ΔG:
minln[met],ΔfG∘′∈CCM1Nexpmet∑(ln[met]exp-ln[met]smet)2+1Nexpfor∑(ΔfGexp∘′-ΔfG∘′sΔfG)2+1Nexprxn∑(ΔGexp-ΔGsΔG)2,
S is the stoichiometric matrix with rows and columns representing individual metabolites and reactions, respectively. ΔG, ΔfG°′, and ln[met] are vectors of free energy of reaction, standard free energy of formation, and log-concentrations. s refer to the standard errors of the measurements or component contribution estimates.
Nexpfor,Nexpmet , and
Nexprxn are the number of input metabolite formation energies, experimentally measured metabolite concentrations and ΔG.
For reactions whose ΔG were not precisely determined, ΔG was constrained to be negative in the direction of net flux. For the eukaryotic cells, ΔfG°′ of TCA metabolites depended on whether they are in cytosol or mitochondria due to pH difference across compartments, and the values of ΔfG°′ calculated for mitochondria were used. Inorganic phosphate concentrations were input as follows: 20 mM in E. coli58 (link); 50 mM in yeast5 (link); and 5 mM in mammalian iBMK cells59 (link). Mitochondrial coenzyme A concentration was input as 5 mM60 (link). The inorganic phosphate and coenzyme A concentrations were allowed to vary within 20% of these values.
Park J.O., Rubin S.A., Xu Y.F., Amador-Noguez D., Fan J., Shlomi T, & Rabinowitz J.D. (2016). Metabolite concentrations, fluxes, and free energies imply efficient enzyme usage. Nature chemical biology, 12(7), 482-489.
Publication 2016
Carbon Cells Cloning Vectors Coenzyme A Cytosol Eukaryotic Cells Mammals Metabolism Mitochondria Phosphates
5
Optimizing Cellular Metabolism through Quadratic Programming
The set of metabolite concentrations ([met]) and reaction free energies (ΔG) associated with central carbon metabolism (CCM; see Supplementary Fig. 4) that best matched i) the directly observed concentrations for measured metabolites ([met]exp) and ii) the observed cellular ΔG for measured reactions (ΔGexp) were computed. An important consideration in this calculation is that literature values for ΔG°′ may themselves contain error. In addition, these ΔG°′ values are interrelated, such that ΔG°′ for any sequence of metabolic reactions must be given by the sum of the formation energies of the products minus the formation energies of the reactants. Accordingly, we set out to optimize both metabolite concentrations and formation energies so as to maximize consistency with prior estimates of ΔfG°′ based on the component contribution method (which itself incorporates prior literature data on ΔG°′) and our experimental observations of metabolite concentrations and cellular reaction free energies. To this end, a quadratic programming problem was formulated with independent variables ln[met] and ΔfG°′, with the optimization objective of minimizing the departure from the expected ΔfG°′ and measured ln[met] and ΔG:
minln[met],ΔfG∘′∈CCM1Nexpmet∑(ln[met]exp-ln[met]smet)2+1Nexpfor∑(ΔfGexp∘′-ΔfG∘′sΔfG)2+1Nexprxn∑(ΔGexp-ΔGsΔG)2,
S is the stoichiometric matrix with rows and columns representing individual metabolites and reactions, respectively. ΔG, ΔfG°′, and ln[met] are vectors of free energy of reaction, standard free energy of formation, and log-concentrations. s refer to the standard errors of the measurements or component contribution estimates.
Nexpfor,Nexpmet , and
Nexprxn are the number of input metabolite formation energies, experimentally measured metabolite concentrations and ΔG.
For reactions whose ΔG were not precisely determined, ΔG was constrained to be negative in the direction of net flux. For the eukaryotic cells, ΔfG°′ of TCA metabolites depended on whether they are in cytosol or mitochondria due to pH difference across compartments, and the values of ΔfG°′ calculated for mitochondria were used. Inorganic phosphate concentrations were input as follows: 20 mM in E. coli58 (link); 50 mM in yeast5 (link); and 5 mM in mammalian iBMK cells59 (link). Mitochondrial coenzyme A concentration was input as 5 mM60 (link). The inorganic phosphate and coenzyme A concentrations were allowed to vary within 20% of these values.
Park J.O., Rubin S.A., Xu Y.F., Amador-Noguez D., Fan J., Shlomi T, & Rabinowitz J.D. (2016). Metabolite concentrations, fluxes, and free energies imply efficient enzyme usage. Nature chemical biology, 12(7), 482-489.
Publication 2016
Carbon Cells Cloning Vectors Coenzyme A Cytosol Eukaryotic Cells Mammals Metabolism Mitochondria Phosphates

Most recents protocols related to «Coenzyme A»

1
Statins Alleviate LS Membrane Remodeling
Not available on PMC !

Example 2

This example demonstrates that statins alleviate LS membrane remodeling phenotypes.

Statins decrease cholesterol (Cho) biosynthesis by inhibiting 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase (FIG. 2A and McFarland et al., Int J Mol Sci 15: 20607-20637 (2014)); consequently, they also down-modulate the downstream synthesis of two intermediates (farnesyl-pyrophosphate and geranyl-geranyl-pyrophosphate) required for RhoA prenylation, which in turn is essential for GTPase membrane anchoring and activation (del Real et al., J Exp Med 200: 541-547 (2004); Demierre et al., Nat Rev Cancer 5: 930-942 (2005); and FIG. 2A). They also have been shown to be active against the RhoA hyperactivation observed in certain cancers (Zhong et al., Cancer Treat Rev 41: 554-567 (2015)).

Several generation statins (Maji et al., Indian J Endocrinol Metab 17: 636-646 (2013)), including fluvastatin, atorvastatin, pitavastatin and rosuvastatin, were tested for their ability to ameliorate LS spreading defects. All statins mitigated to a certain extent the LS spreading phenotype; however, rosuvastatin produced the best results (rosuvastatin>pitavastatin>>>simvastatin and others) in terms of maximizing rescue effect over needed dose and toxicity (FIG. 2B and data not shown).

Phenotype alleviation was observed following the use of an acute rosuvastatin dose (100 μM for 1 h), but similar effect was also evident using lower concentrations (1-10 μM) sustained over longer periods of time (≥72 h; FIG. 2B). Importantly, the latter usage scheme better emulated currently approved treatment conditions with statins that render an effective concentration of free drug in plasma of up to 10 μM (Bjorkhem-Bergman et al., Br J Clin Pharmacol 72: 164-165 (2011)). Following exposure to statins, viability and stress-induced changes in morphology were determined for LS cells (FIG. 2C). Our results showed that rosuvastatin had minimal toxicity, while other statins including pitavastatin and cerivastatin were substantially toxic (FIG. 2C, D). It should be noted that the latter was recalled from the market due to severe rhabdomyolysis effects (Maji et al. (2013), supra). In addition, and to monitor the magnitude of the statins' effects on HMG-CoA reductase in LS cells, we incubated patient fibroblasts in Cho-free media supplemented with vehicle or statins and determined the uptake of fluorescently labeled Cho. While vehicle-treated cells had normal production of endogenous Cho, the ones exposed to statins (due to their HMG-CoA reductase inhibitory activity) were Cho-depleted at a different extent as evidenced by a substantial increase in the uptake of exogenous, fluorescently labeled Cho (FIG. 2E). Our results suggested that rosuvastatin in addition to being less toxic at the chronic dose, led to a less acute inhibition of cholesterol biosynthesis (and consequently to a lower demand of exogenous, fluorescent-analog uptake). However, in contrast with the relatively innocuous chronic exposure (10 μM for ≥72 h), we observed that acute doses of rosuvastatin (100 μM) induced toxicity when exposure time≥15 h (data not shown).

US11857549B2. Compositions and methods for the treatment of Lowe syndrome (2024-01-02). Purdue Research Foundation [US]. Inventors: Ruben Claudio Aguilar [US].
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Patent 2024
Anabolism Atorvastatin Cells cerivastatin Cholesterol cholesterol reductase Coenzyme A farnesyl pyrophosphate Fibroblasts Fluvastatin geranylgeranyl pyrophosphate Guanosine Triphosphate Phosphohydrolases Lanugo Malignant Neoplasms Oculocerebrorenal Syndrome Oxidoreductase Patients Pharmaceutical Preparations Phenotype pitavastatin Plasma Prenylation Psychological Inhibition Rhabdomyolysis RHOA protein, human Rosuvastatin Simvastatin Tissue, Membrane Training Programs
2
Determining Acly Activity in Liver Tissue
Acly activity was determined as described in ref. 59 (link). In brief, liver tissue was lysed in ice-cold 220 mM mannitol, 70 mM sucrose, 5 mM potassium HEPES buffer, pH 7.5 containing 1 mM dithiothreitol. Lysates were centrifuged at 600 × g for 10 min to precipitate the nuclei and debris. Then, the supernatant was centrifuged at 5500 × g for 10 min to precipitate the mitochondrial fraction, and the supernatant was then centrifuged at 20,000 × g for 20 min to generate a cytosolic fraction used to measure enzyme activity. Enzymatic activity was measured in 5 mM citrate, 0.3 mM coenzyme A, 3 mM ATP, 0.15 mM NADH, 10 mM MgCl2, 10 mM dithiothreitol, and 6 units/ml of malate dehydrogenase in 100 mM Tris chloride buffer, pH 8.5 at 37 °C. The NADH disappearance was monitored at 340 nm for 1 min for background, after which 5 mM citrate was added to determine Acly activity.
Sola-García A., Cáliz-Molina M.Á., Espadas I., Petr M., Panadero-Morón C., González-Morán D., Martín-Vázquez M.E., Narbona-Pérez Á.J., López-Noriega L., Martínez-Corrales G., López-Fernández-Sobrino R., Carmona-Marin L.M., Martínez-Force E., Yanes O., Vinaixa M., López-López D., Reyes J.C., Dopazo J., Martín F., Gauthier B.R., Scheibye-Knudsen M., Capilla-González V, & Martín-Montalvo A. (2023). Metabolic reprogramming by Acly inhibition using SB-204990 alters glucoregulation and modulates molecular mechanisms associated with aging. Communications Biology, 6, 250.
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Publication 2023
Buffers Cell Nucleus Chlorides Citrates Coenzyme A Cold Temperature Cytosol Dithiothreitol enzyme activity HEPES Liver Magnesium Chloride Malate Dehydrogenase Mannitol Mitochondria NADH Potassium Sucrose Tissues Tromethamine
3
FICD Activity Assay in CHO Cells
Cells were transfected with 500 ng FICD expression vector, 100 ng SEAP expression vector (UK1014), and 25 ng SV40_Luc_pGL3 expression vector (UK 3075, a transfection marker) per well in 24 well dishes of FICD−/−10 CHO cells. 16 h later the medium was changed and after a further 24 h of culture the medium was collected, heated at 60°C to for 1 h prior to assay for SEAP activity at room temperature by mixing 20 μl of heat‐treated medium to 100 μl 1 M diethanolamine buffer, pH 9.8, 0.5 mM MgCl2 containing 1 mg/ml freshly dissolved phosphatase substrate (4‐Nitrophenyl phosphate disodium salt hexahydrate, Sigma, S0942) and measuring the OD405 and OD 630 every 4.75 min for 20 cycles. The cells were lysed in the dish in 250 μl luciferase lysis buffer (25 mM gly‐gly, 15 mM MgSO4, 4 mM EGTA, 1 mM DTT, 1% Triton X 100) for 20 min on ice and 25 μl was assayed for luciferase activity by addition of 25 μl of luciferase assay reagent (25 mM gly‐gly, 15 mM MgSO4, 4 mM EGTA, 11.7 mM potassium phosphate, 1.6 mM ATP Sigma A2383, 0.2 mg/ml coenzyme A Alfa‐Aesar J65434.MC, 500 μM d‐Luciferin, ABcam ab143655) in a BMG labtech Clariostar plate reader using SMART control v 6.10 acquisition software and MARS v 4.10 data analysis software. ANOVA in Prism software indicated that there was a significant difference amongst means (P < 0.0001) and Šídák's multiple comparisons test was used to determine the significance between data pairs as indicated in the legend. Parallel 6 well dishes were transfected and harvested for immunoblot as in Figs 4 and 5.
Perera L.A., Hattersley A.T., Harding H.P., Wakeling M.N., Flanagan S.E., Mohsina I., Raza J., Gardham A., Ron D, & De Franco E. (2023). Infancy‐onset diabetes caused by de‐regulated AMPylation of the human endoplasmic reticulum chaperone BiP. EMBO Molecular Medicine, 15(3), e16491.
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Publication 2023
4-nitrophenylphosphate Biological Assay Buffers Cells CHO Cells Cloning Vectors Coenzyme A diethanolamine Egtazic Acid Figs Hyperostosis, Diffuse Idiopathic Skeletal Immunoblotting Luciferases Luciferins Magnesium Chloride MAR 10 neuro-oncological ventral antigen 2, human Paragangliomas 3 Phosphoric Monoester Hydrolases potassium phosphate prisma Simian virus 40 Sodium Chloride Sulfate, Magnesium Transfection Triton X-100
4
Doxycycline-Inducible Let-7 Reporter Assay
Human HeLa-rtTA cells expressing reverse tetracycline-controlled transactivator82 (link) were grown in DMEM with GlutaMAX supplement (DMEM + GlutaMAX, Gibco) with 10% FBS and used in luciferase reporter assay. Transfections were done in 96-well plates with PEI using a 1:3 ratio of DNA:PEI. Cells were transfected with 1–3 ng of FL/RL doxycycline-inducible let-7 reporter per well. Increasing amounts of GFP-let-7 sponge (40, 60, 80, 100 and 125 ng per well) were co-transfected, where indicated. GFP-encoding plasmid was used as a filler, to top up each transfection to the same total amount of DNA. Expression of luciferase reporters was induced with doxycycline (1 µg ml−1), and cells were lysed 24 hours after transfection. Luciferase activities were measured with a homemade luciferase reporter assay system as described previously84 (link). More specifically, 45 µl of FLuc reagent (75 mM HEPES pH 8.0, 0.1 mM EDTA, 4 mM MgSO4, 530 µM ATP, 270 µM coenzyme A, 470 µM DTT and 470 µM luciferin) and 45 µl of RLuc reagent (2.2 mM Na2EDTA, 220 mM K3PO4 pH 5.1, 0.44 mg ml−1 of BSA, 1.1 M NaCl, 1.3 mM NaN3 and 0.6 µg ml−1 of coelenterazine) reagents per sample were used to measure luciferase activities.
Mendonsa S., von Kügelgen N., Dantsuji S., Ron M., Breimann L., Baranovskii A., Lödige I., Kirchner M., Fischer M., Zerna N., Bujanic L., Mertins P., Ulitsky I, & Chekulaeva M. (2023). Massively parallel identification of mRNA localization elements in primary cortical neurons. Nature Neuroscience, 26(3), 394-405.
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Publication 2023
Biological Assay Cells coelenterazine Coenzyme A Dietary Supplements Doxycycline Edetic Acid HeLa Cells HEPES Homo sapiens Luciferases Luciferins Plasmids Porifera Sodium Azide Sodium Chloride Sulfate, Magnesium Tetracycline Transfection
5
Citrate Synthase Activity Measurement
Citrate synthase activity in the brown adipose tissue was assayed in approximately 10 mg of brown adipose tissue lysed in 20 volumes of CelLytic MT Cell Lysis containing 1% (v/v) of protease inhibitor cocktail P8340 (Sigma, Saint-Louis, MO, USA) by bead-beating. The lysate was centrifuged two times at 10,000 g during 10 min at 4°C in order to remove the lipids and the tissue debris. Tissue extract was diluted 1:10 in a 100 mM phosphate buffer (pH 7.1) containing 10 mM 5,5′-dithiobis-(2-nitrobenzoic acid) (DTNB) and 30 mM acetyl-CoA. After the addition of 10 mM oxaloacetate, free coenzyme A produced from the condensation of acetyl-CoA and oxaloacetate was bound to DTNB, and resulting change in light absorbance detected spectrophotometrically at 412 nm was used to determine the activity of citrate synthase (µmol/mg/s).
Régnier M., Van Hul M., Roumain M., Paquot A., de Wouters d’Oplinter A., Suriano F., Everard A., Delzenne N.M., Muccioli G.G, & Cani P.D. (2023). Inulin increases the beneficial effects of rhubarb supplementation on high-fat high-sugar diet-induced metabolic disorders in mice: impact on energy expenditure, brown adipose tissue activity, and microbiota. Gut Microbes, 15(1), 2178796.
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Publication 2023
Brown Fat Buffers Citrate (si)-Synthase Coenzyme A Coenzyme A, Acetyl Dithionitrobenzoic Acid Light Lipids Nitrobenzoic Acids Oxaloacetate Phosphates Protease Inhibitors Tissues

Top products related to «Coenzyme A»

1
Coenzyme a by Merck Group
Sourced in United States, Germany
Coenzyme A is a cofactor essential for numerous enzymatic reactions in living organisms. It plays a critical role in the metabolism of carbohydrates, fats, and amino acids. Coenzyme A is widely used in biochemical and pharmaceutical research applications.
2
Adenosine triphosphate (atp) by Merck Group
Sourced in United States, Germany, United Kingdom, China, Sao Tome and Principe, Italy, Japan, Macao, Spain, Canada, France, Switzerland, Ireland, Sweden, Australia
ATP is a laboratory instrument used to measure the presence and concentration of adenosine triphosphate (ATP) in various samples. ATP is a key molecule involved in energy transfer within living cells. The ATP product provides a reliable and accurate method for quantifying ATP levels, which is useful in applications such as microbial detection, cell viability assessment, and ATP-based assays.
3
Acetyl coa by Merck Group
Sourced in United States, Germany, Sao Tome and Principe, China
Acetyl-CoA is a fundamental metabolic intermediate that plays a critical role in various cellular processes. It is the key entry point into the citric acid cycle, a central pathway in cellular respiration and energy production. Acetyl-CoA is involved in the synthesis of fatty acids, cholesterol, and other important biomolecules. It serves as a substrate for a wide range of enzymatic reactions, making it essential for maintaining cellular homeostasis and supporting diverse metabolic functions.
4
Thiamine pyrophosphate by Merck Group
Sourced in United States
Thiamine pyrophosphate is a cofactor for several enzymes involved in carbohydrate metabolism. It is a derivative of the vitamin thiamine (vitamin B1).
5
Triton x 100 by Merck Group
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Triton X-100 is a non-ionic surfactant commonly used in various laboratory applications. It functions as a detergent and solubilizing agent, facilitating the solubilization and extraction of proteins and other biomolecules from biological samples.
6
Coenzyme a trilithium salt by Merck Group
Sourced in United States
Coenzyme A trilithium salt is a laboratory reagent used as a cofactor in enzymatic reactions. It is a salt form of coenzyme A, which is an essential cofactor involved in various metabolic pathways, including the citric acid cycle and fatty acid metabolism. The trilithium salt provides a stable and soluble form of coenzyme A for use in biochemical assays and experiments.
7
Lipofectamine 2000 by Thermo Fisher Scientific
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Lipofectamine 2000 is a cationic lipid-based transfection reagent designed for efficient and reliable delivery of nucleic acids, such as plasmid DNA and small interfering RNA (siRNA), into a wide range of eukaryotic cell types. It facilitates the formation of complexes between the nucleic acid and the lipid components, which can then be introduced into cells to enable gene expression or gene silencing studies.
8
Coenzyme a sodium salt by Merck Group
Sourced in United States
Coenzyme A sodium salt is a chemical compound that serves as an important cofactor in various enzymatic reactions. It is a critical component in the metabolism of carbohydrates, fats, and amino acids, playing a central role in the citric acid cycle. The sodium salt form ensures solubility and stability of the coenzyme.
9
Igepal by Merck Group
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IGEPAL is a nonionic detergent product manufactured by Merck Group. It is primarily used as a surfactant and emulsifier in various laboratory applications. The core function of IGEPAL is to aid in the solubilization, dispersal, and stabilization of materials in aqueous solutions.
10
Bovine serum albumin (bsa) by Merck Group
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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.

More about "Coenzyme A"

Coenzyme A (CoA) is a critical cofactor involved in numerous essential metabolic processes, including energy production, fatty acid synthesis, and the citric acid cycle.
It consists of a pantothenic acid moiety linked to a β-mercaptoethylamine group and an adenosine 5'-diphospho group.
CoA plays a central role in the metabolism of carbohydrates, lipids, and amino acids, and its accurate quantification and study is vital for understanding cellular energetics and regulatory pathways.
Researchers can leverage PubCompare.ai, an AI-driven platform, to optimize their CoA research protocols for reproducibility and accuracy by easily locating and comparing methods from the literature, preprints, and patents to identify the best approaches and products for their experiments.
The AI-powered comparisons on PubCompare.ai can help ensure CoA research is efficient and reliable.
Synonyms for CoA include acetyl-CoA, succinyl-CoA, and malonyl-CoA, while related terms include ATP, thiamine pyrophosphate, Triton X-100, and Coenzyme A trilithium salt.
Researchers may also utilize Lipofectamine 2000, Coenzyme A sodium salt, IGEPAL, and bovine serum albumin in their CoA-related studies.
By leveraging the insights provided by PubCompare.ai, scientists can optimize their CoA research protocols and acheive more reproducible and accurate results.