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Sigma-Aldrich

Acetylcholinesterase Activity Assay Kit

Sinônimo(s):

AChE Assay Kit

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About This Item

Código UNSPSC:
12352202
NACRES:
NA.83

uso

sufficient for 200 colorimetric test

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

Descrição geral

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.

Aplicação

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

Características e benefícios

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!

Definição da unidade

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.

Pictogramas

Corrosion

Palavra indicadora

Danger

Frases de perigo

Declarações de precaução

Classificações de perigo

Eye Dam. 1

Código de classe de armazenamento

10 - Combustible liquids

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


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Narisa Kamkaen et al.
Molecules (Basel, Switzerland), 27(10) (2022-05-29)
L-dopa, a dopaminergic agonist, is the gold standard for the treatment of Parkinson's disease. However, due to the long-term toxicity and adverse effects of using L-dopa as the first-line therapy for Parkinson's disease, a search for alternative medications is an
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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