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Acetylcholinesterase / ACHE Antibody Datasheet
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|Detection limit is 0.00975 ng/well in ELISA|
Acetylcholinesterase / ACHE Antibody Product Information
Recombinant Mouse Acetylcholinesterase / ACHE protein (Catalog#50543-M08H)
|Antibody Type :||Rabbit Polyclonal Antibody ( Antibody Purification Platform )|
|Ig Type :||
|Formulation :||0.2 μm filtered solution in PBS with 5% trehalose|
Produced in rabbits immunized with purified, recombinant Mouse Acetylcholinesterase / ACHE (rM Acetylcholinesterase / ACHE; Catalog#50543-M08H; NP_033729.1; Met 1-Leu 614). Total IgG was purified by Protein A affinity chromatography.
Acetylcholinesterase / ACHE Antibody Usage Guide
Mouse Acetylcholinesterase / ACHE
|Western blot :||This antibody can be used at 1-2 μg/mL with the appropriate secondary reagents to detect Mouse ACHE in WB.|
|Direct ELISA :||This antibody can be used at 0.5-1.0 μg/mL with the appropriate secondary reagents to detect Mouse ACHE. The detection limit for Mouse ACHE is approximately 0.00975 ng/well.|
|Storage :||This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -70℃. Preservative-Free.
Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.
Acetylcholinesterase / ACHE Antibody Related Products & Topics
Acetylcholinesterase / ACHE Antibody Background
Acetylcholinesterase, also known as ACHE, is an enzyme that degrades (through its hydrolytic activity) the neurotransmitter acetylcholine, producing choline and an acetate group. It is mainly found at neuromuscular junctions and cholinergic synapses in the central nervous system, where its activity serves to terminate synaptic transmission. ACHE 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 attachment to the cell surface. ACHE interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers. ACHE has a very high catalytic activity. Each molecule of ACHE degrades about 25000 molecules of acetylcholine per second. The choline produced by the action of ACHE is recycled. It is transported, through reuptake, back into nerve terminals where it is used to synthesize new acetylcholine molecules.
- Wilson M.D. et al., 2001, Nucleic acids Res. 29: 1352-1365.
- Yang L. et al., 2002, Neurosci. Res. 42: 261-268.
- Hillier L.W. et al., 2003, Nature. 424: 157-164.
- Ota T. et al., 2004, Nat. Genet. 36: 40-45.
Acetylcholinesterase / ACHE related areas, pathways, and other information