|Reactivity||Human, Mouse, Rat|
|Calculated MW||67796 Da|
|Positive Control||Western blot: Raji, Jurkat, COS7, NIH3T3 mouse and rat cerebellum lysates|
|Application & Usage||Western blot: ~1:2000|
|Other Names||ACHE; Acetylcholinesterase|
|Formulation||100 µl of antibody in PBS with 0.09% (W/V) sodium azide|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||ACHE Antibody (CT) (Clone 684CT8.3.4) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.|
|Cellular Location||Cell junction, synapse Secreted. Cell membrane; Peripheral membrane protein Isoform H: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side|
|Tissue Location||Isoform H is highly expressed in erythrocytes.|
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Provided below are standard protocols that you may find useful for product applications.
Acetylcholinesterase (AChE) hydrolyzes acetylcholine at synaptic junctions. Alternative mRNA splicing gives rise to three forms of AChE. It plays a role in neuronal apoptosis. The T form, also known as the asymmetric form, is soluble and is present in synapses. The H form is also known as the globular form and is present on the outer surfaces of cell membranes. The R form is not known to be a functional species. AChE globular form subunits are GPI-anchored to cell membranes and asymmetric subunits are anchored to basal lamina components by a collagen tail. The catalytic subunits of AChE are oligomers composed of disulfide-linked homodimers. The loss of AChE from cholinergic and noncholinergic neurons in the brain is seen in patients with Alzheimer’s disease. However, AChE activity is increased around amyloid plaques, which may be due to a disturbance in calcium homeostasis involving the opening of L-type voltage-dependent calcium channels.
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