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Alpha-conotoxin Bt1.8

α-Ctx Bt1.8, Bt1.8

A selective and potent α6/α3β2β3 and α3β2 nAChRs Antagonist

Cat #: STC-020
Alternative Name α-Ctx Bt1.8, Bt1.8
Lyophilized Powder yes
  • Bioassay Tested
  • Origin Conus betulinus
    Source Synthetic peptide
    MW: 1646 Da
    Purity: >98%
    Form Lyophilized Powder
    Effective concentration 5 – 20 nM
    Sequence GCCSNPACILNNPNQC-NH2
    Modifications Cys16 – C-terminal amide
    Disulfide bonds location- Cys2-Cys8, Cys3-Cys16
    Structure
    Molecular formula C63H100N22O22S4
    Activity A potent and selective α6/α3β2β3 and α3β2 nAChRs antagonist
    References-Activity
    1. Ning, H. et al. (2021) J. Neurochem., 159, 90.
    Shipping and storage Shipped at room temperature. Product as supplied can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C. Protect from light and moisture.
    Solubility Soluble in water. It is recommended to prepare fresh solutions in working buffers before use, or aliquot stock solutions reconstituted in distilled water and keep at -20°C. Upon use, dilute the stock solution in the desired working buffer. Prevent repeated thawing and freezing cycles. Centrifuge all product preparations before use (10,000 g for 5 min).
    Storage of solutions Store up to one week at 4°C or up to 6 months at -20°C.
    Our bioassay
    • Alomone Labs α-conotoxin Bt1.8 inhibits α3/β2 nAChR heterologously expressed in Xenopus oocytes.
      Alomone Labs α-conotoxin Bt1.8 inhibits α3/β2 nAChR heterologously expressed in Xenopus oocytes.
      A. Time course of α-conotoxin Bt1.8 (#STC-020) action on α3/β2 nAChR currents, elicited every 50 sec by a transient application of 20 µM ACh, while membrane potential was held at -80 mV. Application of 10 nM (green) and 100 nM (magenta) α-conotoxin Bt1.8 significantly inhibits the currents.
      B. Superimposed traces of α3/β2 nAChR currents evoked by ACh (arrow) after application of control, 10 nM (green) and 100 nM (magenta) α-conotoxin Bt1.8 (taken from the recording in A).
    References - Scientific background
    1. Ning, H. et al. (2021) J. Neurochem., 159, 90.
    2. Zoli, M. et al. (2015) Neuropharmacology, 96, 302.
    3. Gotti, C. et al. (2009) Biochem. Pharmacol., 78, 703.
    4. Levin, E. Det al. (2006) Psychopharmacology 184, 523.
    Scientific background

    α-conotoxin Bt1.8 (Bt1.8) is a 16 amino acid peptidyl toxin originally cloned from the venom duct of the worm-hunting cone snail, Conus betulinus1. This toxin potently and selectively blocks neuronal α6/α3β2β3 and α3β2 nicotinic acetylcholine receptors (nAChRs), with IC50 values of 2.1 nM and 9.4 nM, respectively1. Bt1.8 belongs to the α4/7-CTx subfamily that primarily targets the vertebrate neuronal nAChRs.

    Neuronal nAChRs are a heterogeneous family of ligand-gated cation channels that are expressed throughout the brain and involved in a wide range of physiological and pathophysiological processes. These distinct receptor subtypes have a pentameric structure consisting of a homomeric or heteromeric combination of 12 different subunits (α2–α10, β2–β4)2.

    nAChRs are critically important for neuronal survival and cognitive function, as well as regulation of neurodegenerative diseases, including Alzheimer’s and Parkinson’s. The nAChR subtypes share a common basic structure, but their biophysical and pharmacological properties depend on their subunit composition. Thus, the subunit makeup of the nAChR subtypes is central to understanding their function in the nervous system and for discovering new subtype-selective drugs2-4.

    Target α6/α3β2β3, α3β2 nAChRs
    Peptide Content: 100%
    Last update: 24/03/2022

    α-Conotoxin Bt1.8 (#STC-020) is a highly pure, synthetic, and biologically active peptide toxin

    For research purposes only, not for human use
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