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Alpha-conotoxin BuIA

α-conotoxin BuIA, Conotoxin Bu1.3, BuIA

A Potent α6/α3β2β3 and α3β2 nAChRs Antagonist

Cat #: STC-030
Alternative Name α-conotoxin BuIA, Conotoxin Bu1.3, BuIA
Lyophilized Powder yes
  • Bioassay Tested
  • Origin Conus bullatus (Bubble cone)
    Source Synthetic peptide
    MW: 1311.6 Da
    Purity: >98%
    Form Lyophilized Powder
    Effective concentration 10 – 50 nM
    Sequence GCCSTPPCAVLYC-NH2
    Modifications Cys13 – C-terminal amide
    Disulfide bonds location- Cys2-Cys8, Cys3-Cys13
    Structure
    Molecular formula C54H82N14O16S4
    Activity A potent α6/α3β2β3, α3β2, and α3β4 nAChRs blocker with a unique ability to kinetically discriminate between the β2 and β4-containing receptor subtypes1.
    References-Activity
    1. Azam, L. et al. (2005) J Biol Chem., 280, 80.
    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 BuIA inhibits α3/β2 nAChRs expressed in Xenopus oocytes.
      Alomone Labs α-Conotoxin BuIA inhibits α3/β2 nAChRs expressed in Xenopus oocytes.
      A. Time course of α-Conotoxin BuIA (#STC-030) 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 BuIA 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 BuIA (taken from the experiment in A).
    References - Scientific background
    1. Azam, L. et al. (2005) J Biol Chem., 280, 80.
    2. Chi, S-W. et al. (2006) Biochem. Biophys. Res. Commun., 349, 1228.
    3. Kim, H-W. and McIntosh, J.M. et al. (2012) FASEB J., 26, 4102.
    4. Shiembob, D. L. et al. (2006) Biochemistry, 2006, 45, 11200.
    5. Zoli, M. et al. (2015) Neuropharmacology, 96, 302.
    6. Gotti, C. et al. (2009) Biochem. Pharmacol., 78, 703.
    7. Levin, E. D. et al. (2006) Psychopharmacology, 184, 523.
    Scientific background

    α-conotoxin BuIA is a 13 amino acid peptidyl toxin that was originally isolated from the fish-eating snail, Conus bullatus1. This toxin exhibits strong antagonistic activity at α6/α3β2β3, α3β2, and α3β4 nicotinic acetylcholine receptors (nAChRs) and has the unique ability to kinetically discriminate between the β2 and β4-containing receptor subtypes, as the off-rates are rapid for β2-subunit, but very slow for β4-containing nAChRs. α-Conotoxin BuIA is a member of the A-superfamily of conotoxins and possess an unusual 4/4 disulfide scaffold. This toxin appears to be a valuable probe to distinguish among nAChRs containing different α and β subunits1-4.

    nAChRs are pentameric ligand-gated ion channels that 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 drugs5-7.

    Target α6/α3β2β3, α3β2, and α3β4 nAChRs
    Peptide Content: 100%
    Last update: 05/09/2022

    α-Conotoxin BuIA (#STC-030) is a highly pure, synthetic, and biologically active peptide toxin.

    For research purposes only, not for human use
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