Technical Data
Acetylcholinesterase YT blood group (Acetylcholine acetylhydrolase, ACHE, precursor, ARACHE, N-ACHE-YT)
Cholinergic neurotransmission occurs in motor, autonomic and central nervous synapses and requires very rapid inactivation of its transmitter, acetylcholine (ACh). Acetylcholinesterase (AChE) rapidly hydrolyzes ACh to acetate and choline, thereby inactivating it. AChE is found in the neuromuscular junction anchored to the basal lamina which runs between the nerve terminal and muscle membrane. AChE is also found outside the nervous and neuromuscular system in blood, lymph, germ and liver cells suggesting a role for AChE not related to cholinergic transmission. Another less specific cholinesterase, butyrylcholinesterase (BChE), seems to contribute to the regulation of the ACh concentration in the synaptic cleft.

Suitable for use in ELISA and Western Blot. Other applications not tested.

Recommended Dilution:
ELISA: 1:64000
Western Blot: 0.3-1ug/ml
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot and store at -20C. Aliquots are stable for at least 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
PabAffinity Purified
100ug-20CBlue IceHumanGoat
As reported
Synthetic peptide of ACHE.
Purified by immunoaffinity chromatography.
Supplied as a liquid in Tris-saline, pH 7.2, 0.5% BSA, 0.02% sodium azide.
Recognizes ACHE at ~70kD in human brain lysates. This antibody is expected to recognize isoform NP_000656 only (the ubiquitously expressed, hydrophillic form). Species Crossreactivity: Chicken, mouse, rabbit and rat.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Cottingham MG, Voskuil JL, Vaux DJ. The intact human acetylcholinesterase C-terminal oligomerization domain is alpha-helical in situ and in isolation, but a shorter fragment forms beta-sheet-rich amyloid fibrils and protofibrillar oligomers. Biochemistry. 2003 Sep 16;42(36):10863-73.