Recombinant human Acetylcholinesterase (AChE) is expressed in human HEK 293 cells as a 583 amino acids glycoprotein with a calculated molecular mass of 64.6 kDa. The DTT-reduced protein migrates as a ~70 kDa polypeptide on SDS-PAGE due to glycosylation. This protein is manufactured in human cells, with no serum. The human cells system allows human-like glycosylation and folding, and often supports higher specific activity of the protein. AChE is a serine hydrolase mainly found at neuromuscular junctions and cholinergic brain synapses. AChE, hydrolyzes choline esters. Its principal biological role is the termination of impulse transmission at cholinergic synapses by rapid hydrolysis of the neurotransmitter acetylcholine (ACh) to acetate and choline. Organophosphorus (OP) poisons form a covalent bond with a serine residue at the active site of AChE, and are thus potent irreversible inhibitors of AChE. AChE inhibitors are used in treatment of various neuromuscular disorders3, and have provided the first generation of drugs for the treatment of Alzheimer’s disease. AChE inhibitors inhibit the cholinesterase enzyme from breaking down ACh, increasing both the level and duration of the neurotransmitter action.5 According to the mode of action, AChE inhibitors can be divided into two groups: irreversible and reversible. Reversible inhibitors, competitive or noncompetitive, mostly have therapeutic applications, while toxic effects are associated with irreversible AChE activity modulators. | 
