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Acetylthiocholine

Acetylthiocholine is a synthetic compound used as a substrate for the enzyme acetylcholinesterase, which catalyzes the hydrolysis of the neurotransmitter acetylcholine.
It is commonly utilized in research studies to assess cholinergic function and to measure acetylcholinesterase activity.
Acetylthiocholine has been employed in a variety of experimental settings, including the evaluation of neurotransmitter systems, the investigation of neurological disorders, and the developement of potential therapeutic interventions.
Reserachers can leverage the power of PubCompare.ai's AI-driven platform to optimize their Acetylthiocholine research protocols, effortlessly locating the best protocols from literature, pre-prints, and patents using intelligent comparisons.
PubCompare.ai's platform can guide researchers to the most effective approaches and products for their Acetylthiocholine studies, allowing them to experience the future of research.

Most cited protocols related to «Acetylthiocholine»

1
Acetylcholinesterase Activity Assay Protocol
Cited 7 times
AChE activity was measured using a modified 96-well microplate assay [11] (link) based on Ellman’s method [21] . The enzyme hydrolyses the substrate acetylthiocholine resulting in the product thiocholine which reacts with Ellman’s reagent (DTNB) to produce 2-nitrobenzoate-5-mercaptothiocholine and 5-thio-2-nitrobenzoate which can be detected at 412 nm. 50 mM Tris–HCl pH 8.0 was used as a buffer throughout the experiment unless otherwise stated. AChE used in the assay was from electric eel (type VI-S lyophilized powder, 518 U/mg solid, 844 U/mg protein). The enzyme stock solution (518 U/ml) was kept at −80°C. The further enzyme-dilution was done in 0.1% BSA in buffer. DTNB was dissolved in the buffer containing 0.1 M NaCl and 0.02 M MgCl2. ATCI was dissolved in deionized water. In the 96-well plates, 100 µl of 3 mM DTNB, 20 µl of 0.26 U/ml of AChE, and 40 µl of buffer (50 mM tris pH 8.0), 20 µl of each extract in various concentrations (25, 50, 100, 250 and 500 µg/ml) dissolved in buffer containing not more than 10% methanol were added to the wells. After mixing, the plate was incubated for 15 min (25°C) and then the absorbance was measured at 412 nm in Tecan infinite 200 microplate reader and the readings were used as blank. The enzymatic reaction was initiated by the addition of 20 µl of 15 mM ATCI and the hydrolysis of acetylthiocholine was monitored by reading the absorbance every 5 min for 20 min. Physostigmine was used as positive control. All the reactions were performed in triplicate. The percentage inhibition was calculated as follows:
Where; E is the activity of the enzyme without extract and S is the activity of enzyme with the extract. IC50 value could be calculated from the % inhibition values of different concentrations of each plant extract.
Mathew M, & Subramanian S. (2014). In Vitro Screening for Anti-Cholinesterase and Antioxidant Activity of Methanolic Extracts of Ayurvedic Medicinal Plants Used for Cognitive Disorders. PLoS ONE, 9(1), e86804.
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Publication 2014
2-nitrobenzoate Acetylthiocholine Biological Assay Buffers Dithionitrobenzoic Acid Electric Eel enzyme activity Enzymes Hydrolysis Magnesium Chloride Methanol Pain Physostigmine Plant Extracts Powder Proteins Psychological Inhibition Sodium Chloride Technique, Dilution Thiocholine Tromethamine
2
AChE Inhibitory Activity Assay Protocol
Cited 6 times
The AChE inhibitory activity was measured using the spectrophotometric method developed by Ellman, et al. [61 (link)], with slight modifications as suggested by Rhee, et al. [62 (link)]. Acetylthiocholine was used as the substrate to detect the inhibition of AChE. The reaction mixture contained 40 µL of Buffer C (Tris–HCl, 50 mM, pH 8, containing 0.1 M of sodium chloride and 0.02 M of magnesium chloride hexahydrate), 20 μL of the tested sample solution, 20 µL of AcSCh (15 mM, PBS pH 7.4), and 100 µL of DTNB (3 Mm, dissolved in Buffer C). The mixture was pre-incubated for 3 min at 25 °C. Finally, the enzymatic reaction was started with the addition of 20 µL of 0.5 U/mL AChE (137 U/mg solid) and then incubated at 25 °C for 30 min. The amount of product released was monitored in an EPOCH 2 (BIOTEK ®) microplate reader every 1 min at 405 nm. All reactions were performed in triplicate in a 96-well microplate. Tested sample solutions from the essential oil were made by dissolving 10 mg in 1 mL MeOH. Two more dilutions were included in MEOH (10× dilution) to obtain final concentrations (1000, 100, and 10 ug/mL) of essential oil in MeOH. The IC50 value was calculated by curve fitting of data (non-linear regression analysis, PRISM 8.0.1, GraphPad, San Diego, CA, USA). Donepezil was used as positive control. Any increase in absorbance because of spontaneous hydrolysis of the substrate was corrected by subtracting the absorbance at the end of pre-incubation from the absorbance measured after the addition of the enzyme. The IC50 value was measured from the corresponding rate of the reaction curve with Graph Pad v8.0.1.5.
Valarezo E., Rivera J.X., Coronel E., Barzallo M.A., Calva J., Cartuche L, & Meneses M.A. (2021). Study of Volatile Secondary Metabolites Present in Piper carpunya Leaves and in the Traditional Ecuadorian Beverage Guaviduca. Plants, 10(2), 338.
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Publication 2021
Acetylthiocholine Buffers Dithionitrobenzoic Acid Donepezil Enzymes EPOCH protocol Hydrolysis Magnesium Chloride Oils, Volatile Pain prisma Psychological Inhibition Sodium Chloride Spectrophotometry Technique, Dilution Tromethamine
3
Ellman's Modified Method for AChE Inhibition and Reactivation
Cited 5 times
Ellman’s method was done with slight modifications of the reference [26 (link),27 (link)]. The chemical principle is depicted in Figure 5. A disposable cuvette was consequently filled with 0.4 mL of 0.4 mg/mL DTNB, 25 μL of AChE solution (0.5 μkat in 1 mM acetylthiocholine), 425 μL of PBS, 50 μL of paraoxon in isopropanol or isopropanol alone. The reaction was started by adding 100 μL of acetylthiocholine chloride in a given concentration for assessment of Km and Vmax or 1 mM for toxicological and pharmacological investigations. Absorbance at 412 nm was measured immediately and after one minute. Enzyme activity was calculated estimating extinction coefficient ɛ = 14,150 M−1cm−1. The oxime drugs were tested in a similar protocol. 425 μL of PBS was reduced to 325 μL of PBS. Paraoxon was added in concentration providing 95% inhibition of AChE. Incubation time was set to 10 minutes. After that, 100 μL of oxime reactivator suspended in PBS was injected into the cuvette and kept for another 10 minutes. The reaction was started again by addition of acetylthiocholine.
Pohanka M., Hrabinova M., Kuca K, & Simonato J.P. (2011). Assessment of Acetylcholinesterase Activity Using Indoxylacetate and Comparison with the Standard Ellman’s Method. International Journal of Molecular Sciences, 12(4), 2631-2640.
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Publication 2011
Acetylthiocholine Chlorides Dithionitrobenzoic Acid enzyme activity Extinction, Psychological Isopropyl Alcohol Oximes Pain Paraoxon Pharmaceutical Preparations Psychological Inhibition
4
Acetylcholinesterase Inhibition Assay
Cited 4 times
The inhibition of AChE was measured using the spectrophotometric method developed by Ellman et al. [33 (link)], with slight modifications as suggested by Rhee et al. [34 (link)] and fully detailed for our research group in a previous study [35 (link)]. Briefly, the reaction mixture contained 40μL of Buffer Tris, 20 μL of the tested sample solution, 20 μL of acetylthiocholine (ATCh, 15 mM, PBS pH 7.4), and 100μL of DTNB (3 Mm, Buffer Tris). Pre-incubation was carried out for 3 min at 25°C and continuous shaking. Finally, the addition of 20 μL of 0.5 U/mL AChE started the reaction, and the amount of product released was monitored in an EPOCH 2 (BIOTEK®) microplate reader at 405 nm, 25°C and 60 min.
Sample solutions of EtOH and EtOAc extracts from S. luteus were made by dissolving 10 mg in 1 mL MeOH. Two more dilutions (10 × factor dilution) were included to obtain 1000, 100, and 10 μg/mL final concentrations. All the compounds were tested at a maximum concentration of 250 μM. Progression curves were calculated from absorbance, according to a standard curve of DTNB and L-GSH at different molar concentrations to measure the initial velocity, expressed as mM/min of product released. The corresponding IC50 value was calculated by curve fitting data (linear regression or non-linear regression analysis, PRISM 8.0.1, GraphPad, San Diego, CA, USA). As a protic non-selective solvent, MeOH was selected to dissolve samples and employed as a negative control at a maximum concentration of 10% in the final mix volume without affecting enzyme reaction. Donepezil-hydrochloride was used as a positive control with a calculated IC50 value of 12.40 ± 1.35 nM close to our previous report, as shown by Valarezo et al. [35 (link)].
Andrade J.M., Pachar P., Trujillo L, & Cartuche L. (2022). Suillin: A mixed-type acetylcholinesterase inhibitor from Suillus luteus which is used by Saraguros indigenous, southern Ecuador. PLoS ONE, 17(5), e0268292.
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Publication 2022
Acetylthiocholine Buffers Disease Progression Dithionitrobenzoic Acid Donepezil Hydrochloride Enzymes EPOCH protocol Ethanol Molar Pain prisma Psychological Inhibition Solvents Spectrophotometry Technique, Dilution Tromethamine
5
Enzyme Inhibitory Activities of Pepper Extracts
Cited 3 times
Analysis of AChE and BChE activities were adapted from the method of Jung et al. (2009) (link), with modifications indicated in Kukreja et al. (2018) . The AChE assay mixture contained 20 ng AChE (100 μL), 0.8 mM acetylthiocholine (40 μL), 16 mM 5,5-dithio-bis-(2-nitrobenzoic acid) (DTNB) (10 μL), and the extract (50 μL). Enzyme and substrate were prepared in assay buffer (50 mM KPB, pH 7.0) (50 μL), while DTNB was prepared in methanol. Enzyme inhibitory activity was spectrophotometrically measured at a wavelength of 412 nm using the 96-well microplate reader. Inhibitory activities of pepper extracts were calculated as percentage of inhibition using the equation:
where A is an initial velocity of the reaction with enzyme, a is an initial velocity of the reaction without enzyme, B is an initial velocity of the enzyme reaction with extract, and b is an initial velocity of the reaction with extract but without enzyme.
The BChE assay mixture contained 100 ng BChE in 50 mM KPB, pH 7.0; 1 mM MgCl2 (100 μL); 1 mM butyrylthiocholine in 50 mM KPB, pH 7.0 (40 μL); 16 mM DTNB in 50 mM KPB, pH 7.0 (10 μL); and extract (50 μL). Enzyme inhibitory activity was spectrophotometrically measured at a wavelength of 412 nm using the 96-well microplate reader. Inhibitory activities of pepper extracts were calculated as percentage of inhibition as above.
Since inhibitory activities of AChE and BChE were determined utilizing enzyme kinetics, interferences from sample colors can be unconcerned. Inhibitory activities were determined using the rate of yellow color development during the enzyme assay (which becomes more yellow with time). Therefore, even though the samples had strong colors (yellow, green, red, and orange), the yellow color will only develop in the assay with enzyme. Thus, the yellow color measured in the assay only results from the reaction between the substrate and the enzyme. Eserine, a reversible anti-cholinesterase drug, was used as a control inhibitor for both AChE and BChE assays.
Thuphairo K., Sornchan P, & Suttisansanee U. (2019). Bioactive Compounds, Antioxidant Activity and Inhibition of Key Enzymes Relevant to Alzheimer’s Disease from Sweet Pepper (Capsicum annuum) Extracts. Preventive Nutrition and Food Science, 24(3), 327-337.
Publication 2019
Acetylthiocholine Biological Assay Buffers Butyrylthiocholine Cholinesterase Inhibitors Dithionitrobenzoic Acid enzyme activity Enzyme Assays Enzymes Eserine Kinetics Magnesium Chloride Methanol Nitrobenzoic Acids Pain Pharmaceutical Preparations Piper nigrum Psychological Inhibition

Most recents protocols related to «Acetylthiocholine»

1
Enzymatic Reaction Monitoring via SFME-nanoESI MS
Not available on PMC !

Example 10

For initiating an enzymatic reaction, acetylthiocholine (final concentration of 1.8 mg mL-1) was added into human blood sample, which had been diluted 10 times with phosphate buffered saline (PBS). For experiment producing the data for FIG. 17 panel B, 5 μL blood sample with acetylthiocholine added was loaded into a capillary along with 5 μL extraction solvent. Enzymatic reaction progress was determined by periodically performing the SFME-nanoESI MS analysis of the substrate (m/z 162) and the reaction product thiocholine (m/z 120) (FIG. 18 panels A-B). For each SFME-nanoESI MS analysis, the liquid plugs were pushed to let the extraction solvent reach the capillary tip for spray and then pulled back after the MS analysis. MRM was performed for measuring the intensities of TCh (m/z 120→61) and ATCh (m/z 162→102). The ratios of TCh/ATch are used for making the plot in FIG. 17 panel B. Three replicates were performed for each time point. The standard deviations are marked with the error bars in the FIG. 17 panel B.

US11875983B2. Systems and methods for quantifying an analyte extracted from a sample (2024-01-16). Purdue Research Foundation [US]. Inventors: Zheng Ouyang [US], Yue Ren [IN], Ziqing Lin [US].
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Patent 2024
Acetylthiocholine BLOOD Capillaries Enzymes Homo sapiens Phosphates Saline Solution Solvents Thiocholine
2
Assessing AChE Inhibition by Enriched Fractions
The effect of the enriched fraction on the insect’s acetylcholinesterase enzyme (AChE) was studied following Ellman’s method with slight modification (Ellman, 1959 (link)). The AChE enzyme hydrolyses the substrate acetylthiocholine to produce acetate and thiocholine. Thiocholine reacts with Ellman’s reagent (DTNB) to produce 2-nitrobenzoate-5-mercaptothiocholine and 5-thio-2-nitrobenzoate which can be detected at 412 nm. The enzyme activity was tested against crude enzyme extract of S. oryzae, R. dominica, and T. castaneum in -vitro conditions. The insects (20 adults each) were homogenized using 0.5M Tris-HCl buffer and stored at -200C. For the study, crude enzyme extract was pre-incubated with the enriched fraction and with standard inhibitor (Pyridostigmine bromide) at different doses of 25, 50, 75, and 100 μg/ml of insect’s enzyme extract at 37°C for 30 mins. A microplate reader was used to measure the difference in the absorbance. In a microplate well 200 µl of the reaction mixture, 3 µl of 0.1M acetylthiocholine chloride, 10 µl of insect homogenate, and 87 µl of water were added to make the total volume of 300 µl. The reaction mixture is prepared by adding 10.5 ml of cocktail (13 ml of 1M NaCl, 2 ml 1M MgCl2, 10 ml of 0.5M Tris-HCl, and 10 ml of 0.2M EDTA), 3 ml of 1mM DTNB and 6.5 ml of water in a reagent bottle. The reaction is initiated either by adding the treated enzyme or substrate and expressed as percentage inhibition.
Inhibition (%) = 100 - Change of sample absorbance/Change of blank absorbance X 100
Singh K.D., Koijam A.S., Bharali R, & Rajashekar Y. (2023). Insecticidal and biochemical effects of Dillenia indica L. leaves against three major stored grain insect pests. Frontiers in Plant Science, 14, 1135946.
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Publication 2023
2-nitrobenzoate Acetate Acetylcholinesterase Acetylthiocholine Adult Chlorides Complex Extracts Dithionitrobenzoic Acid Edetic Acid enzyme activity Enzymes Insecta Magnesium Chloride Psychological Inhibition Pyridostigmine Bromide Sodium Chloride Thiocholine Tromethamine
3
Assay of Antioxidant and Enzymatic Activities
Pyrogallol, Catalase, reduced glutathione (GSH), 2,2- diphenyl-1-picrylhydrazyl (DPPH), 1-chloro-2,4-dinitrobenzene (CDNB), Acetylthiocholine chloride, and 5,5-dithio-bis-2-nitrobenzoic acid (DTNB) were procured from Sigma Chemical Co. (St. Louis, MO, USA); hydrogen peroxide, sodium hydroxide, sodium di-hydrogen phosphate, L-ascorbic acid, and sodium carbonate were obtained from Sisco Research Laboratory, Mumbai, India. Sodium Chloride, Magnesium Chloride, and Tris-base were purchased from Himedia Laboratories, Mumbai.
Singh K.D., Koijam A.S., Bharali R, & Rajashekar Y. (2023). Insecticidal and biochemical effects of Dillenia indica L. leaves against three major stored grain insect pests. Frontiers in Plant Science, 14, 1135946.
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Publication 2023
Acetylthiocholine Ascorbic Acid Catalase Chlorides Dinitrobenzenes diphenyl Hydrogen Magnesium Chloride Nitrobenzoic Acids Peroxide, Hydrogen Pyrogallol Reduced Glutathione sodium carbonate Sodium Chloride Sodium Hydroxide sodium phosphate Tromethamine
4
Electrochemical Biosensor for Insecticide Detection
Screen-printed carbon electrodes (SPCEs) were custom-made from Botan Technology Co., Ltd. (Weihai, China). Potassium ferricyanide (K3[Fe(CN)6]) and potassium ferrocyanide (K4[Fe(CN)6]·3H2O) were purchased from Guangfu Technology Development Co., Ltd. (Tianjin, China). Potassium chloride (KCl), sodium dihydrogen phosphate (NaH2PO4·2H2O) and disodium hydrogen phosphate (Na2HPO4·12H2O) were purchased from Sinopharm Chemical Reagent Beijing Co., Ltd. (Beijing, China). Graphene (GR) and Au nanoparticles (AuNPs) were purchased from Jiangsu Xianfeng Nanomaterials Technology Co., Ltd. (Nanjing, China). Nafion (10 wt% in H2O) was purchased from Maclean Biochemical Technology Co., Ltd. (Shanghai, China). Acetylcholinesterase (AChE, 2 KU), acetylthiocholine chloride (ATCl), isocarbophos (ICP) were purchased from Sigma Aldrich (USA). All other chemicals and reagents used in this study were of analytical grade, and all aqueous solutions were prepared with ultrapure water (18.25 MΩ cm−1) by a Millipore Direct-Q water system.
Wen L., Wang J., Liu Z., Tao C.A., Rao J., Hang J, & Li Y. (2023). A portable acetylcholinesterase-based electrochemical sensor for field detection of organophosphorus. RSC Advances, 13(10), 6389-6395.
Publication 2023
Acetylcholinesterase Acetylthiocholine Carbon Chlorides Graphene isocarbophos Nafion Pain potassium ferricyanide potassium ferrocyanide sodium phosphate, dibasic sodium phosphate, monobasic
5
Enzymatic Assays for Aquatic Biomonitoring
For acetylcholinesterase (AChE) measurement, samples from head and tail were used. The head was considered from mouth until operculum and tail were considered from anal pore until caudal fin tip. For the measurement of glutathione-S-transferase (GST) activity, gill and body samples were used. We took body samples, considering from operculum until anal pore. For LDH, only samples from the tail were used. The samples were stored in phosphate buffer 0.1 M, pH 7.2, at −20 °C. Samples were defrosted on ice, triturated using scissors, homogenized using a sonicator, and centrifuged while refrigerated (4 °C) for 20 min at 10,000 g. The resulting post-mitochondrial supernatant (PMS) was isolated and placed in 96-well microplates for enzymatic determinations performed spectrophotometrically (Thermo, Waltham, MA, USA) in quadruplicate.
The Bradford method was used to quantify proteins [30 (link)]. The reactions were performed spectrophotometrically in quadruplicate, with the protocol adapted for microplates [31 (link)].
AChE activity was carried out using acetylthiocholine (ASCh) and propionylthiocoline (PSCh) as substrates. We followed the protocol described by Ellman and coworkers [32 (link)], with modifications (absorbance at 414 nm, every 40 s, for 5 min). AChE was expressed as nanomol of substrate hydrolyzed per minute and per mg of protein (U) after 10 min of absorbance reaction for measurement of enzymatic activity. Lactate Dehydrogenase (LDH) activity was performed using pyruvate as substrate and measuring the reduction of pyruvate and the oxidation of NADH at 340 nm, every 40 s, for 5 min. The determinations of the LDH activity followed the protocol described by Vassault [33 ]. The variations in Glutathione-S-Transferase (GST) activity were carried out according to the method of Habig and coworkers [34 (link)].
de Souza Freire I., Fascineli M.L., Piau T.B., Pereira B.F, & Grisolia C.K. (2023). Multilevel Toxicity Evaluations of Polyethylene Microplastics in Zebrafish (Danio rerio). International Journal of Environmental Research and Public Health, 20(4), 3617.
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Publication 2023
Acetylcholinesterase Acetylthiocholine Anus Buffers enzyme activity Enzymes Gills Glutathione S-Transferase Head Human Body Lactate Dehydrogenase Mitochondria NADH Opercular Cortex Oral Cavity Phosphates Proteins Pyruvates Tail

Top products related to «Acetylthiocholine»

1
Acetylthiocholine by Merck Group
Sourced in United States, Germany, Italy, Israel
Acetylthiocholine is a synthetic compound used as a substrate in the measurement of acetylcholinesterase activity. It is a colorless, crystalline solid that is soluble in water and organic solvents. Acetylthiocholine is commonly used in biochemical and pharmacological research applications.
2
5 5 dithiobis 2 nitrobenzoic acid by Merck Group
Sourced in United States, Germany, India, China, Italy, United Kingdom, Japan, Spain, Israel, Canada, Argentina
5,5′-dithiobis(2-nitrobenzoic acid) is a chemical compound used in various laboratory applications. It is a solid, crystalline substance with a specific chemical structure and formula. The primary function of this compound is to serve as a reagent in analytical and biochemical procedures, without further interpretation of its intended use.
3
5 5 dithiobis 2 nitrobenzoic acid dtnb by Merck Group
Sourced in United States, Germany, China, Italy, India, Switzerland, Spain, United Kingdom, Sao Tome and Principe
5,5′-dithiobis(2-nitrobenzoic acid) (DTNB) is a chemical compound used in various laboratory applications. It is a water-soluble, yellow-colored reagent that is commonly employed for the determination of thiol groups in proteins and other biological samples.
4
Acetylcholinesterase by Merck Group
Sourced in United States, Germany, Italy, Chile, Spain
Acetylcholinesterase is an enzyme that catalyzes the breakdown of the neurotransmitter acetylcholine in the synaptic cleft. It is an important component in the regulation of nerve impulse transmission.
5
Acetylthiocholine chloride by Merck Group
Sourced in United States
Acetylthiocholine chloride is a chemical compound used in laboratory settings. It is a substrate for the enzyme acetylcholinesterase, which is commonly used to measure enzymatic activity. The compound is primarily utilized in assays and experimental protocols involving the analysis of cholinergic systems and neurotransmitter function.
6
Donepezil by Merck Group
Sourced in United States, Germany, Italy, Japan, France
Donepezil is a laboratory equipment product manufactured by Merck Group. It is designed to assist in various research and analytical applications. The core function of Donepezil is to provide a reliable and consistent performance in the tasks it is intended for.
7
Dimethyl sulfoxide (dmso) by Merck Group
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DMSO is a versatile organic solvent commonly used in laboratory settings. It has a high boiling point, low viscosity, and the ability to dissolve a wide range of polar and non-polar compounds. DMSO's core function is as a solvent, allowing for the effective dissolution and handling of various chemical substances during research and experimentation.
8
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.
9
2 2 diphenyl 1 picrylhydrazyl (dpph) by Merck Group
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DPPH is a chemical compound used as a free radical scavenger in various analytical techniques. It is commonly used to assess the antioxidant activity of substances. The core function of DPPH is to serve as a stable free radical that can be reduced, resulting in a color change that can be measured spectrophotometrically.
10
Epoch 2 by Agilent Technologies
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The Epoch 2 is a high-performance microplate reader offered by Agilent Technologies. It is designed to perform absorbance, fluorescence, and luminescence measurements in a variety of microplate formats. The Epoch 2 provides accurate and reliable data for a range of life science applications.

More about "Acetylthiocholine"

Acetylthiocholine is a synthetic compound widely used in research to study cholinergic function and measure acetylcholinesterase activity.
It serves as a substrate for the enzyme acetylcholinesterase, which catalyzes the hydrolysis of the neurotransmitter acetylcholine.
Acetylthiocholine has been employed in a variety of experimental settings, including the evaluation of neurotransmitter systems, the investigation of neurological disorders, and the development of potential therapeutic interventions.
Researchers can leverage the power of PubCompare.ai's AI-driven platform to optimize their Acetylthiocholine research protocols, effortlessly locating the best protocols from literature, pre-prints, and patents using intelligent comparisons.
The platform can also guide researchers to the most effective approaches and products for their Acetylthiocholine studies, allowing them to experience the future of research.
In addition to Acetylthiocholine, other related compounds and techniques are commonly used in this area of research. 5,5′-dithiobis(2-nitrobenzoic acid) (DTNB), also known as Ellman's reagent, is frequently used to measure acetylcholinesterase activity.
Acetylcholinesterase is the enzyme responsible for the hydrolysis of acetylcholine, and it plays a crucial role in the regulation of cholinergic neurotransmission.
Acetylthiocholine chloride is another commonly used substrate for acetylcholinesterase assays.
Donepezil, a medication used to treat Alzheimer's disease, is known to inhibit acetylcholinesterase, thereby increasing the availability of acetylcholine in the brain.
DMSO (dimethyl sulfoxide) is often used as a solvent for various compounds in research studies, including those involving Acetylthiocholine.
Bovine serum albumin (BSA) is a common protein used in assays to stabilize enzymes and proteins, while DPPH (2,2-diphenyl-1-picrylhydrazyl) is a free radical scavenging compound used to evaluate antioxidant activity.
By understanding the broader context and related terms, researchers can more effectively design and conduct their Acetylthiocholine studies, leveraging the insights and tools provided by platforms like PubCompare.ai to optimize their research protocols and drive scientific discoveries.