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United States (US)

AChE blocking peptide

Cat. No. GTX89580-PEP

Species

 Human
Package
100 μg ($239)

APPLICATION

Product Note

The peptide was used in the production of GTX89580.

PROPERTIES

Form

Lyophilized powder

Buffer

Reconstitute with 200μl distilled water to obtain a 0.5mg/ml peptide solution. Lyophilized from 5% (v/v) acetonitrile/H₂O.

Preservative

No preservative

Storage

Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.

Region/Sequence

QFDHYSKQDRCSDL

Note

For laboratory research use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.

Purchasers shall not, and agree not to enable third parties to, analyze, copy, reverse engineer or otherwise attempt to determine the structure or sequence of the product.

TARGET

Synonyms

Acetylcholinesterase (Cartwright Blood Group) , Acee , Arache , N-Ache , Yt , Ache

Background

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, Jul 2008]

Research Area

REFERENCE

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REVIEW

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Package List Price ($)
$ 239