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C1682 Sigma

Acetylcholinesterase human

recombinant, expressed in HEK 293 cells, lyophilized powder, ≥1,000 units/mg protein (Lowry)

Synonym: AChE, Acetylcholine acetylhydrolase



Analysis Note

The activity obtained using acetylcholine as substrate is 30-100 times that obtained with butyrylcholine, using acetylcholinesterase from electric eel.

Biochem/physiol Actions

Major degradative enzyme for acetylcholine in vivo. Converts acetylcholine + H2O to choline + acetic acid.


0.1 mg in serum bottle

Unit Definition

One unit will hydrolyze 1.0 μmole of acetylcholine to choline and acetate per min at pH 8.0 at 37 °C

Physical form

This product is supplied as a lyophilized powder. Lyophilized from 0.22 μm filtered solution in PBS, pH7.4.

General description

Recombinant human Acetylcholinesterase (AChE) is expressed in human HEK 293 cells as a 583 amino acids glycoprotein with a calculated molecular mass of 64.6 kDa. The DTT-reduced protein migrates as a ~70 kDa polypeptide on SDS-PAGE due to glycosylation. This protein is manufactured in human cells, with no serum. The human cells expression system allows human-like glycosylation and folding, and often supports higher specific activity of the protein.

AChE is a serine hydrolase mainly found at neuromuscular junctions and cholinergic brain synapses.1 AChE, hydrolyzes choline esters. 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.1

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.2

AChE inhibitors are used in treatment of various neuromuscular disorders3, and have provided the first generation of drugs for the treatment of Alzheimer’s disease.4

AChE inhibitors inhibit the cholinesterase enzyme from breaking down ACh, increasing both the level and duration of the neurotransmitter action.5 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.5

Price and Availability

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Safety Information

NONH for all modes of transport
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Protocols & Articles

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers


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