AchE (N-Term) antibody

Details for Product No. ABIN965502
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Antigen
Epitope
N-Term
(14), (4), (4), (3), (2), (2), (1), (1), (1), (1), (1), (1)
Reactivity
Human
(37), (23), (22), (2)
Host
Rabbit
(33), (5), (2)
Clonality
Polyclonal
Application
Immunohistochemistry (IHC)
(38), (17), (9), (6), (3), (1)
Pubmed 4 references available
Quantity 0.1 mg
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Catalog No. ABIN965502
288.75 $
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Immunogen Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to N-terminal residues of human ACHE (N-terminal extended acetylcholinesterase)
Purification Purified by antigen-specific affinity chromatography.
Background ACHE(acetylcholinesterase) rapidly hydrolyzes choline released into the synapse. ACHE interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers. ACHE is responsible for the Yt blood group system. The molecular basis of the Yt(a)=Yt1/ Yt(b)=Yt2 blood group antigens is a single variation in position 353, His-353 corresponds to Yt(a) and the rare variant with Asn-353 to Yt(b).
Application Notes ELISA, Western blotting: 1µg/ml for 2hrs.
Restrictions For Research Use only
Format Liquid
Buffer This antibody is stored in PBS, 50% glycerol
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Product cited in: Shafferman, Kronman, Flashner et al.: "Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding." in: The Journal of biological chemistry, Vol. 267, Issue 25, pp. 17640-8, 1992 (PubMed).

Velan, Grosfeld, Kronman et al.: "The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase Cys-580----Ala mutant." in: The Journal of biological chemistry, Vol. 266, Issue 35, pp. 23977-84, 1992 (PubMed).

Soreq, Ben-Aziz, Prody et al.: "Molecular cloning and construction of the coding region for human acetylcholinesterase reveals a G + C-rich attenuating structure." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 87, Issue 24, pp. 9688-92, 1991 (PubMed).

Meshorer, Toiber, Zurel et al.: "Combinatorial complexity of 5' alternative acetylcholinesterase transcripts and protein products." in: The Journal of biological chemistry, Vol. 279, Issue 28, pp. 29740-51, 2004 (PubMed).

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