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Merck

CS0003

Sigma-Aldrich

Acetylcholinesterase Activity Assay Kit

Sinónimos:

AChE Assay Kit

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About This Item

UNSPSC Code:
12352202

usage

sufficient for 200 colorimetric test

shipped in

dry ice

storage temp.

−20°C

Categorías relacionadas

General description

The Acetylcholinesterase Activity Assay Kit (Colorimetric) provides a simple, quick, and direct procedure for measuring Acetylcholinesterase levels in a variety of samples such as serum, plasma, tissues or cell lysates / cell extracts. This assay is based on the Ellman method in which thiocholine, produced by Acetylcholinesterase, reacts with DTNB 5,5¢-dithiobis (2-nitrobenzoic acid) to form a colorimetric product (412 nm), proportional to the Acetylcholinesterase activity present. This kit does not require weighing, or mixing of multiple reagents. The Acetylcholinesterase activity is measured without the use of a calibration curve. The Acetylcholinesterase Positive Control in the kit can be used to screen for Acetylcholinesterase inhibitors.

The detection range: 10-600 units/liter of Acetylcholinesterase activity.
The detection time: 5-10 minutes

Acetylcholinesterase ( AChE) is a serine hydrolase found at neuromuscular junctions and cholinergic brain synapses. AChE, hydrolyzes choline esters. Acethlcholinesterase activity is related to the function of the nerve response. Its principal biological role is the termination of impulse transmission at cholinergic synapses by rapid hydrolysis of the neurotransmitter acetylcholine (ACh) to acetate and choline.

Organophosphorus (OP) poisons form a covalent bond with a serine residue at the active site of AChE, and are thus potent irreversible inhibitors of AChE.

AChE inhibitors are used in treatment of various neuromuscular disorders, and have provided the first generation of drugs for the treatment of Alzheimer′s disease.

AChE inhibitors inhibit the cholinesterase enzyme from breaking down ACh, increasing both the level and duration of the neurotransmitter action According to the mode of action, AChE inhibitors can be divided into two groups: irreversible and reversible. Reversible inhibitors, competitive or noncompetitive, mostly have therapeutic applications, while toxic effects are associated with irreversible AChE activity modulators.

Application

Detection of Acetylcholinesterase activity levels in a variety of samples such as serum and plasma, tissues or cell lysates
Enables to screen for Acetylcholinesterase inhibitors

Features and Benefits

Our economical Acetylcholinesterase (AChE) Activity Kit also saves your time and efforts:

  • A simple, quick, sensitive, and direct procedure for measuring Acetylcholinesterase Activity levels in a variety of samples such as serum and plasma, tissues or cell lysates enables to screen for Acetylcholinesterase inhibitors
  • Supportive calculator (Click here to download a calculator excel file): Will calculate the reagents needed according to your experimental needs, and analyses your results based on your experimental data!

Unit Definition

One unit of Acetylcholinesterase is the amount of enzyme that catalyzes the production of 1.0 mmole of thiocholine per minute at pH 8.0 at room temperature. This kit contains sufficient reagents for 200 tests.

pictograms

Corrosion

signalword

Danger

hcodes

Hazard Classifications

Eye Dam. 1

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Molecules (Basel, Switzerland), 27(10) (2022-05-29)
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Neuromuscular transmission -enzymatic destruction of acetylcholine
Barnard, E.A. et al.
SpringerPlus, 201-224 (1974)
Anticholinesterase agents
Taylor, P. et al.
Goodman and Gilman?s The Pharmacological Basis of Therapeutics, 201-216 (2006)
Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states
Daniel M. Quinn et al.
Chemical Reviews, 955-979 (1987)

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