Search results for: Amplite™ Colorimetric Acetylcholinesterase Assay Kit
#37129743 2023/05/02 To Up
Toxicity, Pharmacokinetic Profile, and Compound-Protein Interaction Study of Polygonum minus Huds Extract.
Several phytochemicals with potential for bioactivity can be found in Polygonum minus (PM). The goal of this investigation was to establish the minimally toxic dose of PM for pharmaceutical use. To explain the stability and reactivity of the compounds under study, the lowest unoccupied molecular orbital (LUMO), the highest occupied molecular orbital (HOMO), and the natural bond orbital were all combined. Additionally, the cytotoxicity of the aqueous and ethanolic extract of PM on the (Hs888Lu) cell line was determined using the MTS Assay Kit (cell proliferation) (colorimetric). The hematological, hepatic, and renal functions were examined during the acute toxicity test on Sprague Dawley rats. SwissADME and ADMET were used to investigate the absorption, distribution, metabolism, excretion, and toxicity (ADMET) of the chemicals isolated from PM, including gallic acid, quercetin, rutin, and coumaric acid (PMCs). Molecular docking was used to examine the inhibitory effect against human H/K ATPase, cyclooxygenase-2, and acetylcholinesterase. The outcomes indicated that neither the aqueous nor the ethanolic extract of PM is harmful. The development of plant-based medicine was made possible by the phenolic chemicals, primarily quercetin and rutin, which exhibit a considerable binding affinity to human H/K ATPase, cyclooxygenase-2, and acetylcholinesterase.Suhailah Wasman Qader, Mehmet Ozdemir, Innocent Benjamin, Chioma M Chima, A Suvitha, Jaquline Chinna Rani, Terkumbur E Gber, Gugan Kothandan
2159 related Products with: Toxicity, Pharmacokinetic Profile, and Compound-Protein Interaction Study of Polygonum minus Huds Extract.
1 Set1 Set1 Set1 Set1 Set1 Set1 Set1 Set1 Set1 Set1 Set1 SetRelated Pathways
#30830739 2019/03/14 To Up
Protein-Inorganic Hybrid Nanoflower-Rooted Agarose Hydrogel Platform for Point-of-Care Detection of Acetylcholine.
Rapid and precise profiling of acetylcholine (ACh) has become important for diagnosing diseases and safeguarding health care because of its pivotal role in the central nervous system. Herein, we developed a new colorimetric sensor based on protein-inorganic hybrid nanoflowers as artificial peroxidase, comprising a test kit and a smartphone reader, which sensitively quantifies ACh in human serum. In this sensor, ACh indirectly triggered the substrate reaction with the help of a multienzyme system including acetylcholinesterase, choline oxidase, and mimic peroxidase (nanoflowers), accompanying the enhancement of absorbance intensity at 652 nm. Therefore, the multienzyme platform can be used to detect ACh via monitoring the change of the absorbance in a range from 0.0005 to 6.0 mmol L. It is worth mentioning that the platform was used to prepare a portable agarose gel-based kit for rapid qualitative monitoring of ACh. Coupling with ImageJ program, the image information of test kits can be transduced into the hue parameter, which provides a directly quantitative tool to identify ACh. Based on the advantages of simple operation, good selectivity, and low cost, the availability of a portable kit for point-of-care testing will achieve the needs of frequent screening and diagnostic tracking.Deshuai Kong, Rui Jin, Xu Zhao, Hongxia Li, Xu Yan, Fangmeng Liu, Peng Sun, Yuan Gao, Xishuang Liang, Yuehe Lin, Geyu Lu
2574 related Products with: Protein-Inorganic Hybrid Nanoflower-Rooted Agarose Hydrogel Platform for Point-of-Care Detection of Acetylcholine.
100ug1 g10ìg5 ml100 mg2x96 well plate10 mg1mg0.1 mg100μg100testsRelated Pathways
#29462698 2018/02/17 To Up
Piper sarmentosum Roxb. confers neuroprotection on beta-amyloid (Aβ)-induced microglia-mediated neuroinflammation and attenuates tau hyperphosphorylation in SH-SY5Y cells.
Piper sarmentosum Roxb. (PS), belonging to Piperaceae family, is an edible plant with medicinal properties. It is traditionally used by the Malays to treat headache and boost memory. Pharmacological studies revealed that PS exhibits anti-inflammatory, anti-oxidant, anti-acetylcholinesterase, and anti-depressant-like effects. In view of this, the present study aimed to investigate the anti-inflammatory actions of PS and its potential neuroprotective effects against beta-amyloid (Aβ)-induced microglia-mediated neurotoxicity.Emilia Tze Ying Yeo, Kelly Wang Ling Wong, Mun Ling See, Ka Yan Wong, Sook Yee Gan, Elaine Wan Ling Chan
2475 related Products with: Piper sarmentosum Roxb. confers neuroprotection on beta-amyloid (Aβ)-induced microglia-mediated neuroinflammation and attenuates tau hyperphosphorylation in SH-SY5Y cells.
96 tests 100ul96 tests96 tests96 tests100ug96 tests100 μg100ug100ug LyophilizedRelated Pathways
#18555983 2008/05/03 To Up
Advantages of the WRAIR whole blood cholinesterase assay: comparative analysis to the micro-Ellman, Test-mate ChE, and Michel (DeltapH) assays.
Red blood cell AChE (RBC-AChE) and plasma BChE can be used as sensitive biomarkers to detect exposure to OP nerve agents, pesticides, and cholinergic drugs. In a comparative study, RBC-AChE and serum BChE activities in whole blood was obtained from forty seven healthy male and female human volunteers, and then exposed separately ex vivo to three OP nerve agents (soman (GD), sarin (GB) and VX) to generate a wide range of inhibition of AChE and BChE activity (up to 90% of control). These samples were measured using four different ChE assays: (i) colorimetric microEllman (using DTNB at 412 nm), (ii) Test-mate ChE field kit (also based on the Ellman assay), (iii) Michel (delta pH), and (iv) the Walter Reed Army Institute of Research Whole Blood (WRAIR WB) cholinesterase assay. The WRAIR assay is a modified Ellman method using DTP at 324 nm (which minimizes hemoglobin interference and improves sensitivity), and determines AChE and BChE in a small whole blood sample simultaneously. Scatter plots of RBC-AChE activities were determined using the WRAIR ChE assay versus the micro-Ellman, Test-mate and Michel after exposure to varying concentrations of soman, sarin and VX. Regression analyses yielded mostly linear relationships with high correlations (r2 = 0.83-0.93) for RBC-AChE values in the WRAIR assay compared to the alternate methods. For the plasma BChE measurements, individual human values were significantly more variable (as expected), resulting in lower correlations using WRAIR ChE versus the alternate assays (r2 values 0.5 - 0.6). To circumvent the limitations of simple correlation analysis, Bland and Altman analysis for comparing two independent measurement techniques was performed. For example, a Bland and Altman plot of the ratio of the WRAIR whole blood AChE and Michel AChE (plotted on the y-axis) vs. the average of the two methods (x-axis) shows that the majority of the individual AChE values are within +/- 1.96 S.D. of the mean difference, indicating that the two methods may be used interchangeably with a high degree of confidence. The WRAIR ChE assay can be thus be used as a reliable inter-conversion assay when comparing results from laboratory-based (Michel) and field-based (Test-mate ChE kit), which use different methodology and report in different units of AChE activity.Julian R Haigh, Lee J Lefkowitz, Benedict R Capacio, Bhupendra P Doctor, Richard K Gordon
2668 related Products with: Advantages of the WRAIR whole blood cholinesterase assay: comparative analysis to the micro-Ellman, Test-mate ChE, and Michel (DeltapH) assays.
100 assays100 assays100 assays100 assays100 assays100 assays25 assaysRelated Pathways
#10928685 // To Up
Acetyl- and pseudo-cholinesterase activities of plasma, erythrocytes, and whole blood in male beagle dogs using Ellman's assay.
Organophosphate and carbamate ester insecticides, main causes of pesticide poisoning, inhibit cholinesterase (ChE) enzymes. The aim of this study was to measure and compare baseline values for pseudocholinesterase and acetylcholinesterase (AChE) enzyme activities of different blood fractions in the dog to aid in diagnosis of anticholinesterase poisoning. After collecting blood samples from 23 6-24-mo-old male beagle dogs, Ellman's colorimetric assay was run on plasma, red blood cells (RBC), and whole blood fractions prepared in triplicate. The procedure described in a commercially available kit was applied to plasma and RBC. Hemolyzed whole blood fractions (final dilution 1:8) avoided the time-consuming and laborious separation of plasma and RBC. In addition to the kit substrate acetylthiocholine (ASCh), we used butyrylthiocholine (BSCh) as substrate. Whatever the substrate, ChE activity was lower in RBC than in other blood preparations. It was higher when using ASCh rather than BSCh as substrate (mean IU/L+/-SD): 563+/-144 and 303+/-45 respectively, in contrast to plasma (1640+/-310 and 2510+/-450). Whole blood enzyme activity did not differ significantly according to substrate: ASCh, 1590+/-190; BSCh, 1620+/-250) with a 2 to 3% within-day coefficient of variation. Enzyme activity was significantly lower in dogs <1-y old. This study confirms the low ChE activity in dog RBC compared to other species and other blood fractions. It shows that using whole blood instead of separating RBC from plasma minimizes the variability of ChE activity in the hemoglobin-rich fraction.M Kolf-Clauw, S Jez, C Ponsart, I S Delamanche
2327 related Products with: Acetyl- and pseudo-cholinesterase activities of plasma, erythrocytes, and whole blood in male beagle dogs using Ellman's assay.
96T900 tests96T10 mg1 mg50 ug 100ug400Tests10 mg100ugRelated Pathways
#9169060 // To Up
Simulated dermal contamination with capillary samples and field cholinesterase biomonitoring.
The extensive international use of organophosphorus compounds (OP) results in numerous acute intoxications each year. OPs inhibit acetylcholinesterase, the enzyme responsible for breaking down the neurotransmitter acetylcholine. The World Health Organization recognizes cholinesterase (ChE) biomonitoring as a preventive measure against OP overexposure. The aim of this study was to determine if dermal OP contamination could interfere with current field ChE biomonitoring assays, which use a fingerstick blood sample. In this study we also sought to determine if high levels of a plasma enzyme, A-esterase, could protect ChE from inhibition by hydrolyzing environmentally generated oxons potentially present in a fingerstick sample. A heparinized venous blood sample was collected from a volunteer. Erythrocyte acetylcholinesterase (AChE) and plasma butyrylcholinesterase (PChE) activities were measured using a field-based colorimetric cholinesterase kit. ChE dose-response curves were constructed by allowing 10-microliters blood samples to contact environmentally realistic levels of OP thioate and oxon for 10 s. An inhibition threshold could not be established for PChE when exposed to oxon within the time necessary to perform a fingerstick analysis. AChE was also inhibited by trace amounts of oxon consistent with previously reported environmental levels. These findings suggest that the reliability of field-based biomonitoring results is limited if OP residues remain on a skin surface at the time of sample collection. A-esterase's role in protecting ChE activity was investigated using capillary and venous blood from 30 unexposed individuals. Baseline ChE activities were measured, as were individual A-esterase activities using paraoxon, diazoxon, and phenylacetate as substrates. Results were then compared to ChE activities measured after 10 s of contact with an environmentally realistic amount of OP, containing 1% oxon. Both ChE activities were significantly inhibited, with capillary values being significantly more inhibited than their venous counterparts. However, no protective effect could be associated between the degree of A-esterase activity and the subsequent level of ChE inhibition observed in an individual's blood. These results suggest that (1) if there is any uncertainty about OP skin contamination, venous blood would be a more appropriate specimen to employ when using field ChE biomonitoring kits--it is collected in larger volumes and has essentially no direct contact to dermal surfaces; and (2) A-esterase activity demonstrates no protective effect against ChE inhibition upon a blood droplet's brief contact with an OP residue containing traces of oxon.K L Yuknavage, R A Fenske, D A Kalman, M C Keifer, C E Furlong
1115 related Products with: Simulated dermal contamination with capillary samples and field cholinesterase biomonitoring.
100 SamplesEach16 Arrays/Slide10 mg96 Samples1 kit(96 Wells)50 ugRelated Pathways
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