
CAS 9000-81-1
:Acetylcholinesterase
Description:
Acetylcholinesterase (AChE) is a crucial enzyme that plays a vital role in the nervous system by catalyzing the hydrolysis of the neurotransmitter acetylcholine into acetate and choline. This process is essential for terminating synaptic transmission, thereby regulating muscle contraction and various neural functions. AChE is a serine hydrolase and is found in various tissues, including the brain, red blood cells, and neuromuscular junctions. The enzyme operates optimally at physiological pH and temperature, exhibiting high specificity for acetylcholine. Its activity can be inhibited by certain compounds, including organophosphates and carbamates, which can lead to toxic effects and are the basis for some insecticides and nerve agents. AChE is also a target for therapeutic agents in conditions such as Alzheimer's disease, where its inhibition can enhance cholinergic signaling. The enzyme's structure typically includes a catalytic triad and a peripheral anionic site, contributing to its function and interaction with inhibitors. Overall, AChE is integral to maintaining proper neurotransmission and is a significant focus in both pharmacology and toxicology.
Formula:Unspecified
Synonyms:- E.C. 3.1.1.7
- Acetylcholinesterase
- Acetylcholine esterase
- Esterase, acetylcholine
- Acetylthiocholinesterase
Sort by
Purity (%)
0
100
|
0
|
50
|
90
|
95
|
100
Found 2 products.
Acetylcholinesterase
CAS:<p>Acetylcholinesterase (ACHE) is an enzyme found at neuromuscular junctions and cholinergic-type chemical synapses, useful in biosensor research.</p>Color and Shape:SolidAcetylcholinesterase, type VI-S, 200-1,000 units/mg protein
CAS:<p>Acetylcholinesterase is an enzyme that breaks down acetylcholine</p>Purity:Min. 95%Color and Shape:Powder


