Acetylcholinesterase (AChE) (N-Term) antibody

Antigen: Acetylcholinesterase (AChE)

Synonyms: YT, ARACHE, N-ACHE, mE1a, mE1b, mE1c, mE1d, mE1e, mE1d', mE1c-long, ACE, AChE, AcChE, CHE, DmAChE, FBgn0000024, dAChE, l(3)26, l(3)87Ed, DmelCG17907, CG17907, zgc:92550, ACHE, Ache, GB14873, dsim_GLEANR_4292, Dsim\GD20515, GD20515, arache, n-ache, ache

Binding Site: N-Term

Clonality: Polyclonal

Host: Rabbit

Reactivity: Human

Conjugate: Un-conjugated

Application: Immunohistochemistry (IHC)

Catalog no.: ABIN965502

Additional Information

Alternative name: ACHE

Immunogen: Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to N-terminal residues of human ACHE (N-terminal extended acetylcholinesterase)

Description: 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).

Synonyms: YT, ARACHE, N-ACHE, mE1a, mE1b, mE1c, mE1d, mE1e, mE1d', mE1c-long, ACE, AChE, AcChE, CHE, DmAChE, FBgn0000024, dAChE, l(3)26, l(3)87Ed, DmelCG17907, CG17907, zgc:92550, ACHE, Ache, GB14873, dsim_GLEANR_4292, Dsim\GD20515, GD20515, arache, n-ache, ache

Application Details

Application Notes: ELISA, Western blotting: 1µg/ml for 2hrs.

Purification: Purified by antigen-specific affinity chromatography.

Buffer: This antibody is stored in PBS, 50% glycerol

Preservative: 0.01% Sodium Azide

Storage: Store at -20°C.

Restrictions: For Research Use only

Publications

Product: 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).