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AChE Antibodies

Santa Cruz Biotechnology, Inc. offers a broad range of AChE antibodies. Select AChE antibodies from several monoclonal and/or polyclonal AChE antibodies listed below. View detailed AChE antibody specifications by linking to the specific product blocks. Select appropriate AChE antibodies for your research by isotype, epitope, applications and species reactivity. AChE gene silencer products in siRNA, shRNA Plasmid and shRNA Lentiviral Particle formats are also available.

Introducing HOVERcruz™,

a unique system for rapid identification of AChE Antibodies. Hover over product names in the table to see representative data for each product.

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Our live chat system is available to answer your product and ordering questions.

See AChE Inhibitors for functional analysis of cellular responses to AChE.

PRODUCT NAMECAT. #ISOTYPEEPITOPEAPPLICATIONSSPECIESCITATIONSRATING
AChE (E-19)sc-6432goat IgGN-terminus (m)WB, IP, IF, ELISAm, r18
AChE (H-134)sc-11409rabbit IgG481-614 (h)WB, IP, IF, ELISAm, r, h, e, c, b, p7
AChE (A-11)sc-373901mouse IgG2a481-614 (h)WB, IP, IF, ELISAhuman
AChE (C-16)sc-6430goat IgGC-terminus (h)WB, IF, ELISAm, r, h, e, c, b, p6
AChE (N-19)sc-6431goat IgGN-terminus (h)WB, IP, IF, ELISAh, r, p13

AChE siRNA, shRNA Plasmid and shRNA Lentiviral Particles gene silencers include:

siRNAsshRNA PlasmidsshRNA Lentiviral ParticlesCITATIONSRANKING
AChE siRNA (h): sc-29628AChE shRNA Plasmid (h):
sc-29628-SH
AChE shRNA (h)
Lentiviral Particles: sc-29628-V
AChE siRNA (m): sc-29629AChE shRNA Plasmid (m):
sc-29629-SH
AChE shRNA (m)
Lentiviral Particles: sc-29629-V

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.