Description
ACHE Antibody | 63-244 | Gentaur UK, US & Europe Distribution
Host: Rabbit
Reactivity: Human
Homology: Predicted species reactivity based on immunogen sequence: Guinea Pig
Immunogen: This ACHE antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 147-175 amino acids from the N-terminal region of human ACHE.
Research Area: Neuroscience
Tested Application: WB, IHC-P, IF, Flow
Application: For WB starting dilution is: 1:1000
For IHC-P starting dilution is: 1:10~50
For FACS starting dilution is: 1:10~50
For IF starting dilution is: 1:10~50
Specificiy: N/A
Positive Control 1: N/A
Positive Control 2: N/A
Positive Control 3: N/A
Positive Control 4: N/A
Positive Control 5: N/A
Positive Control 6: N/A
Molecular Weight: 68 kDa
Validation: N/A
Isoform: N/A
Purification: This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis
Clonality: Polyclonal
Clone: N/A
Isotype: Rabbit Ig
Conjugate: Unconjugated
Physical State: Liquid
Buffer: Supplied in PBS with 0.09% (W/V) sodium azide.
Concentration: batch dependent
Storage Condition: Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Alternate Name: Acetylcholinesterase, AChE, 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. The Protein 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. 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.