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.
C1682
Acetylcholinesterase human
recombinant, expressed in HEK 293 cells, lyophilized powder, ≥1,000 units/mg protein (BCA)
Sinónimos:
AChE, Acetylcholine acetylhydrolase
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| A ustedes/SKU | Disponibilidad | Precio |
|---|---|---|
10 μg | Disponible para enviar HOYdesdeMILWAUKEE | $465.00 |
0.1 mg | Disponible para enviar HOYdesdeMILWAUKEE | $1,220.00 |
Acerca de este artículo
Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.32
EC Number:
232-559-3
MDL number:
Specific activity:
≥1,000 units/mg protein (BCA)
Recombinant:
expressed in HEK 293 cells
Servicio técnico
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Permítanos ayudarleGeneral 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.
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Este artículo | |||
|---|---|---|---|
| description recombinant, expressed in HEK 293 cells, lyophilized powder, ≥1,000 units/mg protein (BCA) | description Type V-S, lyophilized powder, ≥1,000 units/mg protein | description recombinant, ≥10 U/mg, expressed in HEK 293 cells | description Type VI-S, lyophilized powder, 200-1,000 units/mg protein |
| specific activity ≥1,000 units/mg protein (BCA) | specific activity ≥1,000 units/mg protein | specific activity ≥10 U/mg | specific activity 200-1,000 units/mg protein |
| Gene Information human ... ACHE(43) | Gene Information - | Gene Information - | Gene Information - |
| recombinant expressed in HEK 293 cells | recombinant - | recombinant expressed in HEK 293 cells | recombinant - |
| form lyophilized powder | form lyophilized powder | form lyophilized powder | form lyophilized powder |
| storage temp. −20°C | storage temp. −20°C | storage temp. −20°C | storage temp. −20°C |
| mol wt 64.6 kDa | mol wt 280 kDa | mol wt calculated mol wt 138 kDa (The protein migrates as a 180 kDa protein on SDS-PAGE due to glycosylation) | mol wt 280 kDa |
Clase de almacenamiento
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Is there information available about the glycosylation pattern of the recombinant human acetylcholinesterase (product number C1682) expressed in HEK 293 cells?
1 answer-
Helpful?
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