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Acetylcholinesterase antibody (AChE) (N-Term)

Details for Product anti-AChE Antibody No. ABIN965502, Supplier: Login to see
Antigen
  • ACE2
  • Ache
  • GB14873
  • ACHE
  • ACE
  • Dsim\\GD20515
  • GD20515
  • dsim_GLEANR_4292
  • arache
  • n-ache
  • ache
  • ACEE
  • ARACHE
  • N-ACHE
  • YT
  • mE1a
  • mE1b
  • mE1c
  • mE1c-long
  • mE1d
  • mE1d'
  • mE1e
  • zgc:92550
Epitope
N-Term
34
17
10
5
5
5
5
4
4
4
3
3
3
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
Reactivity
Human
171
62
56
42
13
3
3
2
1
1
1
1
1
1
Host
Rabbit
146
57
34
10
Clonality
Polyclonal
Conjugate
This Acetylcholinesterase antibody is un-conjugated
20
11
8
1
1
1
1
1
1
1
1
1
1
1
1
Application
Immunohistochemistry (IHC)
172
128
37
32
29
22
13
11
10
8
6
5
4
3
2
1
1
1
Supplier
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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.
Alternative Name ACHE (AChE Antibody Abstract)
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).
Pathways
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: 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).

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).

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).

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).