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µ-Conotoxin BuIIIA

A Selective and Potent Blocker of NaV1.2 and NaV1.4 Channels

Cat #: STC-540
Lyophilized Powder yes
  • Bioassay Tested
  • Origin Synthetic peptide
    MW: 2752 Da.
    Purity: >98% (HPLC)
    Effective concentration 100 nM – 1 µM.
    Modifications Disulfide bonds between Cys5-Cys16, Cys6-Cys22, and Cys12-Cys23. Cysteine23-C-terminal amidation.
    Molecular formula C106H172N44O31S6.
    Activity µ-Conotoxin BuIIIA is a potent blocker of voltage-gated NaV1.2 and NaV1.4 channels.1
    1. Holford, M. et al. (2009) Toxicon 53, 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.
    Solubility Any aqueous buffer. Centrifuge all product preparations before use (10000 x g 5 min).
    Storage of solutions Up to two weeks at 4°C or three months at -20°C.
    Our bioassay
    • Alomone Labs µ-Conotoxin-BuIIIA blocks NaV1.4 channel current expressed in Xenopus oocytes.
      Alomone Labs µ-Conotoxin-BuIIIA blocks NaV1.4 channel current expressed in Xenopus oocytes.
      A. Time course of µ-Conotoxin-BuIIIA (#STC-540) inhibition of NaV1.4 channel currents. Membrane potential was held at -100 mV and current was elicited by a 120 ms voltage step to 0 mV, delivered every 10 sec. 100 nM BuIIIA, applied for 8 min, as indicated by the bar (green), significantly inhibited the current. B. Superimposed traces of NaV1.4 currents upon application of control (black) and of 100 nM BuIIIA (green), taken from the recording shown in A.
    References - Scientific background
    1. Yao, S. et al. (2008) Biochemistry 47, 10940.
    2. Kuang, Z. et al. (2013) ACS Chem. Biol. 8, 1344.
    3. Holford, M. et al. (2009) Toxicon 53, 90.
    Scientific background

    μ-Conotoxins (μ-CTX) are peptide toxins that block voltage-gated Na+ channels (VGSCs), which are responsible for the influx of Na+ ions during action potentials in excitable tissues1.

    µ-Conotoxin BuIIIA is originally isolated from the venom of the cone snail Conus bullatus and acts as a selective and potent blocker of voltage-gated NaV1.2 and NaV1.4 channels. The conotoxin inhibits Na+ flux by blocking the Na+ channel pore.

    BuIIIA is considered to be part of a novel class of μ-conopeptides discovered from a newly defined class of fish-hunting cone snails, the Textilia clade. In addition, Conus bullatus peptides help define a new branch of the M-superfamily of conotoxins, namely M-5 due to a unique N-terminal extension. This N-terminus also exists in µ-Conotoxin BuIIIB and BuIIIC but absent in all other μ-conotoxins2,3.

    µ-Conotoxin BuIIIA is used to determine the structure-activity relationship of voltage-gated Na+ channels3.

    Target NaV1.2, NaV1.4 channels
    Net Peptide Content: 100%
    Last update: 24/01/2021

    µ-Conotoxin BuIIIA (#STC-540) is a highly pure, synthetic, and biologically active peptide toxin.

    For research purposes only, not for human use
    Shipping and Ordering information