Product Description
ACHE Antibody | 18-820 | ProSci
Host: Rabbit
Reactivity: Human, Mouse, Rat
Homology: N/A
Immunogen: Recombinant fusion protein containing a sequence corresponding to amino acids 398-617 of human ACHE (NP_056646.1) .
Research Area: Neuroscience
Tested Application: WB, IHC
Application: WB: 1:500 - 1:2000
IHC: 1:50 - 1:100
Specificiy: N/A
Positive Control 1: SH-SY5Y
Positive Control 2: SGC996
Positive Control 3: Mouse brain
Positive Control 4: Mouse spinal cord
Positive Control 5: Mouse liver
Positive Control 6: Rat spinal cord
Molecular Weight: Observed: 75kDa
Validation: N/A
Isoform: N/A
Purification: Affinity purification
Clonality: Polyclonal
Clone: N/A
Isotype: IgG
Conjugate: Unconjugated
Physical State: Liquid
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Concentration: N/A
Storage Condition: Store at -20˚C. Avoid freeze / thaw cycles.
Alternate Name: ACHE, YT, acetylcholinesterase (YT blood group) , ACEE, ARACHE, N-ACHE
User Note: Optimal dilutions for each application to be determined by the researcher.
BACKGROUND: 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.