|Reactivity||Human, Mouse, Rat|
|Description||Rabbit IgG polyclonal antibody for Acetylcholinesterase(ACHE) detection. Tested with WB in Human;Mouse;Rat.|
|Reconstitution||Add 0.2ml of distilled water will yield a concentration of 500ug/ml.|
|Other Names||Acetylcholinesterase, AChE, 126.96.36.199, ACHE|
|Calculated MW||67796 MW KDa|
|Application Details||Western blot, 0.1-0.5 µg/ml, Human, Mouse, Rat|
|Subcellular Localization||Cell junction, synapse . Secreted . Cell membrane ; Peripheral membrane protein .|
|Tissue Specificity||Isoform H is highly expressed in erythrocytes. .|
|Contents||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.|
|Immunogen||A synthetic peptide corresponding to a sequence at the C-terminus of human ACHE (592-614aa SSYMVHWKNQFDHYSKQDRCSDL), different from the related mouse and rat sequences by one amino acid.|
|Purification||Immunogen affinity purified.|
|Cross Reactivity||No cross reactivity with other proteins|
|Storage||At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing.|
|Sequence Similarities||Belongs to the type-B carboxylesterase/lipase family.|
|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.
ACHE is also known as Acetylcholinesterase. And 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.
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