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United States (US)

AChR beta 3 blocking peptide

Cat. No. GTX88687-PEP

Species

Human
Package
100 μg ($239)

APPLICATION

Product Note

The peptide was used in the production of GTX88687.

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

C-SRHVKKEHFISQ

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

Cholinergic Receptor Nicotinic Beta 3 Subunit , Chrnb3

Background

The nicotinic acetylcholine receptors (nAChRs) are members of a superfamily of ligand-gated ion channels that mediate fast signal transmission at synapses. The nAChRs are (hetero)pentamers composed of homologous subunits. The subunits that make up the muscle and neuronal forms of nAChRs are encoded by separate genes and have different primary structure. There are several subtypes of neuronal nAChRs that vary based on which homologous subunits are arranged around the central channel. They are classified as alpha-subunits if, like muscle alpha-1 (MIM 100690), they have a pair of adjacent cysteines as part of the presumed acetylcholine binding site. Subunits lacking these cysteine residues are classified as beta-subunits (Groot Kormelink and Luyten, 1997 [PubMed 9009220]). Elliott et al. (1996) [PubMed 8906617] stated that the proposed structure for each subunit is a conserved N-terminal extracellular domain followed by 3 conserved transmembrane domains, a variable cytoplasmic loop, a fourth conserved transmembrane domain, and a short C-terminal extracellular region.[supplied by OMIM, Apr 2010]

Research Area

REFERENCE

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REVIEW

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Package List Price ($)
$ 239