*Optimal dilutions/concentrations should be determined by the researcher.
Not tested in other applications.
Raji , mouse brain , rat brain
Bovine, Cat, Guinea pig, Rhesus Monkey(>80% identity)
1XPBS pH7, 20% Glycerol
0.025% ProClin 300
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
1.81 mg/ml (Please refer to the vial label for the specific concentration.)
Recombinant protein encompassing a sequence within the C-terminus region of human AChE. The exact sequence is proprietary.
Purified by antigen-affinity chromatography.
For laboratory research use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Purchasers shall not, and agree not to enable third parties to, analyze, copy, reverse engineer or otherwise attempt to determine the structure or sequence of the product.
acetylcholinesterase (Cartwright blood group) , ACEE , ARACHE , N-ACHE , YT
Cell junction , synapse , Secreted , Cell membrane; Peripheral membrane protein , Isoform T: Nucleus , Isoform H: Cell membrane; Lipid-anchor , GPI-anchor; Extracellular side , Cell junction , synapse , Secreted , Cell membrane , Isoform T: Nucleus , Isof
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. [provided by RefSeq]