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Acetylcholinesterase - AChE

Target Class Non-Kinase Enzymes FamilyCholinesterase
SpeciesHuman   
Background
Acetylcholinesterase hydrolyzes the neurotransmitter, acetylcholine at neuromuscular junctions and brain cholinergic synapses, and thus terminates signal transmission. It is also found on the red blood cell membranes, where it constitutes the Yt blood group antigen. Acetylcholinesterase exists in multiple molecular forms which possess similar catalytic properties, but differ in their oligomeric assembly and mode of cell attachment to the cell surface. It is encoded by the single ACHE gene, and the structural diversity in the gene products arises from alternative mRNA splicing, and post-translational associations of catalytic and structural subunits. The major form of acetylcholinesterase found in brain, muscle and other tissues is the hydrophilic species, which forms disulfide-linked oligomers with collagenous, or lipid-containing structural subunits. The other, alternatively spliced form, expressed primarily in the erythroid tissues, differs at the C-terminal end, and contains a cleavable hydrophobic peptide with a GPI-anchor site. It associates with the membranes through the phosphoinositide (PI) moieties added post-translationally. [provided by RefSeq, Jul 2008]

Protein Source
Human(recombinant):Expressed in CHO cells
Readout
Enzymatic activity
Method
Detect conversion of acetylthiocholine to thiocholine using DTNB
Substrate
Acetylthiocholine
Agonist Effect (Activation)
insufficient information
Antagonist Effect (Inhibition)
decrease BP; decrease HR; increase GI motility (decrease at high doses); brochoconstriction; increase respiratory secretions
Ref.
Bowes et. al. 2012
AntagonistIC50(nM)
Galanthamine390
Physostigmine 12
Enzyme and test compound are preincubated for 15 minutes at room temp before substrate addition. Acetylthiocholine and DTNB are added and incubated at room temperature for 30 minutes. Signal is detected by measuring absorbance at 405 nm.
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