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C1682

Sigma-Aldrich

Acetylcholinesterase human

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

Synonym(s):

AChE, Acetylcholine acetylhydrolase

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

recombinant

expressed in HEK 293 cells

Quality Level

form

lyophilized powder

specific activity

≥1,000 units/mg protein (Lowry)

mol wt

64.6 kDa

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... ACHE(43)

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Acetylcholinesterase from human erythrocytes as a surrogate biomarker of lead induced neurotoxicity
Gupta VK, et al.
Enzyme Research, 2015 (2015)
Sebastian Oddsson et al.
Molecules (Basel, Switzerland), 25(12) (2020-06-26)
Despite extensive efforts in the development of drugs for complex neurodegenerative diseases, treatment often remains challenging or ineffective, and hence new treatment strategies are necessary. One approach is the design of multi-target drugs, which can potentially address the complex nature
Different cholinesterase inhibitor effects on CSF cholinesterases in Alzheimer patients
Nordberg A, et al.
Current Alzheimer Research, 6(1), 4-14 (2009)
In vitro effect of H 2 O 2, some transition metals and hydroxyl radical produced via fenton and fenton-like reactions, on the catalytic activity of AChE and the Hydrolysis of ACh
Mendez-Garrido A, et al
Neurochemical Research, 39(11), 2093-2104 (2014)
Acetylcholinesterase Inhibitors: Pharmacology and Toxicology
Mirjana B C, et al.
Current Neuropharmacology, 11(3), 315-335 (2013)

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