Goat polyclonal antibody raised against synthetic peptide of ACHE.
Immunogen:
A synthetic peptide corresponding to human ACHE.
Sequence:
QFDHYSKQDRCSDL
Host:
Goat
Theoretical MW (kDa):
67.8
Reactivity:
Human
Specificity:
This antibody is expected to recognize isoform NP_000656 only (the ubiquitously expressed, hydrophillic form).
Form:
Liquid
Purification:
Antigen affinity purification
Concentration:
0.5 mg/mL
Quality Control Testing:
Antibody Reactive Against Synthetic Peptide.
Recommend Usage:
ELISA (1:64000) Western Blot (0.3-1 ug/mL) The optimal working dilution should be determined by the end user.
Storage Buffer:
In Tris saline, pH 7.3 (0.5% BSA, 0.02% sodium azide)
Storage Instruction:
Store at -20°C. Aliquot to avoid repeated freezing and thawing.
Note:
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Publication Reference
1.
Cholinergic imbalance in the multiple sclerosis hippocampus. Kooi EJ, Prins M, Bajic N, Belien JA, Gerritsen WH, van Horssen J, Aronica E, van Dam AM, Hoozemans JJ, Francis PT, van der Valk P, Geurts JJ.Acta Neuropathol. 2011 Jun 21. [Epub ahead of print]
ACHE polyclonal antibody (Cat # PAB6747) (0.3 ug/mL) staining of human brain (Hippocampus) lysate (35 ug protein in RIPA buffer) with (A) and without (B) blocking with the immunising peptide. Primary incubation was 1 hour. Detected by chemiluminescence.
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