raised against amino acids 574-583 of AChE of human origin
recommended for detection of brain AChE of human origin by WB and IP; non cross-reactive with AChE from erythrocytes; also reactive with additional species, including bovine
AChE Background Information Acetylcholinesterase (AChE) hydrolyzes acetylcholine at synaptic junctions. Alternative mRNA splicing gives rise to three forms of AChE. 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 sununits 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.
AChE (4E11)
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AChE (4E11): sc-80614. Western blot analysis of AChE expression in 293T (A) and SW-13 (B) whole cell lysates.
