|Application ||WB, E|
|Other Accession||Q29499, P23795, NP_000656|
|Calculated MW||67796 Da|
|Antigen Region||582-610 aa|
|Other Names||Acetylcholinesterase, AChE, ACHE|
|Target/Specificity||This ACHE antibody is generated from mice immunized with a KLH conjugated synthetic peptide between 582-610 amino acids from the C-terminal region of human ACHE.|
|Format||Mouse monoclonal antibody supplied in crude ascites with 0.09% (W/V) sodium azide.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||ACHE Antibody (C-term) (Ascites) 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 hydrolyzes the neurotransmitter, acetylcholine at neuromuscular junctions and brain cholinergic synapses, and thus terminates signal transmission. It is also found on the red blood cell membranes, where it constitutes the Yt blood group antigen. Acetylcholinesterase exists in multiple molecular forms which possess similar catalytic properties, but differ in their oligomeric assembly and mode of cell attachment to the cell surface. It is encoded by the single ACHE gene, and the structural diversity in the gene products arises from alternative mRNA splicing, and post-translational associations of catalytic and structural subunits. The major form of acetylcholinesterase found in brain, muscle and other tissues is the hydrophilic species, which forms disulfide-linked oligomers with collagenous, or lipid-containing structural subunits. The other, alternatively spliced form, expressed primarily in the erythroid tissues, differs at the C-terminal end, and contains a cleavable hydrophobic peptide with a GPI-anchor site. It associates with the membranes through the phosphoinositide (PI) moieties added post-translationally.
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)
Howard, T.D., et al. Environ. Health Perspect. 118(10):1395-1399(2010)
Cadieux, C.L., et al. Chem. Biol. Interact. 187 (1-3), 229-233 (2010) :
Ruano, G., et al. Pharmacogenomics 11(7):959-971(2010)
Ohno, K., et al. Proc. Natl. Acad. Sci. U.S.A. 95(16):9654-9659(1998)
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