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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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10 μG
$399.71
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10 μG
$399.71
0.1 MG
$1,049.94

About This Item

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

$399.71

List Price$434.00Save 8%
Web-Only Promotion

Estimated to ship onJuly 16, 2025FromMILWAUKEE


Request a Bulk Order

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)

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This Item
C0663SAB4200839C2888
Gene Information

human ... ACHE(43)

Gene Information

human ... ACHE(43)

Gene Information

human ... ACHE(43)

Gene Information

-

specific activity

≥1,000 units/mg protein (Lowry)

specific activity

≥500 units/mg protein (BCA)

specific activity

-

specific activity

≥1,000 units/mg protein

recombinant

expressed in HEK 293 cells

recombinant

-

recombinant

-

recombinant

-

form

lyophilized powder

form

buffered aqueous solution

form

buffered aqueous solution

form

lyophilized powder

mol wt

64.6 kDa

mol wt

~80 kDa

mol wt

-

mol wt

280 kDa

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

General description

Acetylcholinesterase (AChE) is a serine hydrolase,[1] which belongs to the carboxyl esterase family of enzymes.[2] AChE is localised at neuromuscular junctions and cholinergic brain synapses.[1]

Application

Acetylcholinesterase human has been used:
  • as a standard protein to measure protein levels acetylcholinesterase AChE-R and AChE-S[3]
  • to stimulate human fibroblasts[4]
  • to study its in vitro catalytic activity and to determine the effects of metals, H2O2 and OH radicals on the activity[5]

Biochem/physiol Actions

Acetylcholinesterase (AChE) is regarded as a biomarker in neurotoxicity.[2] It is a modulator of nitric oxide signal transduction pathway and marker of membrane integrity and aging.[6] 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.[1]
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

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Questions

  1. Is there information available about the glycosylation pattern of the recombinant human acetylcholinesterase (product number C1682) expressed in HEK 293 cells?

    1 answer
    1. Characterizing the glycosylation pattern of this enzyme is not within the scope of product evaluation in the laboratory. Unfortunately, there is no access to the specific publication containing the details. However, based on the abstract description, the publication "Gene. 1992 Nov 16;121(2):295-304" provides information about the glycosylation patterns of both the dimeric and monomeric forms of recombinant hAChE (rehAChE) expressed in the embryonal kidney 293 cell line, which may be helpful for reference. The PMID for the publication is 1446827.

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