ACHE(CT) (clone 684CT8.3.4), anti-human, mouse, rat antibody
€275.00
In stock
SKU
AC-ABV11257-100
Catalog Number: AC-ABV11257-100
Size: 100 µl
Host: Mouse IgG
Applications: WB
Datasheet
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Size: 100 µl
Host: Mouse IgG
Applications: WB
Datasheet
Request Information
Background:
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.
Other Names:
ACHE, Acetylcholinesterase
Primary Accession: P22303
Gene Name: ACHE
Gene ID: 43
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.
Other Names:
ACHE, Acetylcholinesterase
Primary Accession: P22303
Gene Name: ACHE
Gene ID: 43
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