Acetylcholinesterase human (C15-1289-698)

General description

Acetylcholinesterase (AChE) is a serine hydrolase, which belongs to the carboxyl esterase family of enzymes. AChE is localised at neuromuscular junctions and cholinergic brain synapses.

Application

Acetylcholinesterase human has been used:

• as a standard protein to measure protein levels acetylcholinesterase AChE-R and AChE-S
• to stimulate human fibroblasts
• to study its in vitro catalytic activity and to determine the effects of metals, H₂O₂ and OH radicals on the activity

Biochem/physiol Actions

Acetylcholinesterase (AChE) is regarded as a biomarker in neurotoxicity. It is a modulator of nitric oxide signal transduction pathway and marker of membrane integrity and aging. AChE, hydrolyzes choline esters. It terminates the impulse transmission at cholinergic synapses. AChE does this by rapid hydrolysis of the neurotransmitter acetylcholine (ACh) to acetate and choline. AChE inhibitors prevent the cholinesterase enzyme from breaking down ACh and increases the level and duration of the neurotransmitter action.

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

Unit Definition

One unit will hydrolyze 1.0 μmole of acetylthiocholine to thiocholine and acetate per minute 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 50mM phosphate buffer pH8.

Analysis Note

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