AChe Antibody

INQUIRY

CAT. NO.: AMA-0177

Product Details
Size	100 μL
Reactivity	Human
Host	Rabbit
Source/Isotype	Rabbit IgG
Storage	Store at -20°C.
Purification	This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.

Usage
Application	WB, IHC, IF, FACS
Product Usage Information Dilution	Western Blotting (1:1000); Immunofluorescence (1:10-1:50); Immunohistochemistry (1:10-1:50); Flow Cytometry (1:10–1:50)

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.

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.

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