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Merck

C1682

Sigma-Aldrich

Acetylcholinesterase human

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

Szinonimák:

AChE, Acetylcholine acetylhydrolase

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

CAS-szám:
Enzyme Commission szám:
EC-szám:
MDL-szám:
UNSPSC kód:
12352204
NACRES:
NA.32

rekombináns

expressed in HEK 293 cells

Minőségi szint

form

lyophilized powder

specifikus aktivitás

≥1,000 units/mg protein (Lowry)

molekulatömeg

64.6 kDa

UniProt elérési szám

tárolási hőmérséklet

−20°C

Géninformáció

human ... ACHE(43)

Általános leírás

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.

Alkalmazás

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

Biokémiai/fiziológiai hatások

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.

Egység definíció

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

Fizikai forma

This product is supplied as a lyophilized powder. Lyophilized from 0.22 μm filtered solution in 50mM phosphate buffer pH8.

Analízis megjegyzés

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

Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 3

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

Már rendelkezik ezzel a termékkel?

Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

Jiayi Liu et al.
Frontiers in plant science, 12, 720816-720816 (2021-08-31)
Essential oils (EOs) are often the source of insecticidal substances of high efficiency and low toxicity. From gas chromatograph-mass spectrometer, column chromatography, and nuclear magnetic resonance spectra analyses, twenty terpenes were identified from the EOs of Artemisia nakaii. These comprised
Agneta Nordberg et al.
Current Alzheimer research, 6(1), 4-14 (2009-02-10)
The current study aimed to compare the effects of different cholinesterase inhibitors on acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) activities and protein levels, in the cerebrospinal fluid (CSF) of Alzheimer disease (AD) patients. AD patients aged 50-85 years were randomized to
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)
Acetylcholinesterase from human erythrocytes as a surrogate biomarker of lead induced neurotoxicity
Gupta VK, et al.
Enzyme Research, 2015 (2015)

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