Merck, C1682-10UG, Acetylcholinesterase human

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.
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.
Other Notes
One unit will hydrolyze 1.0 μmole of acetylthiocholine to thiocholine and acetate per minute at pH 8.0 at 37 °C.