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Pandinotoxin Kα

Potassium channel toxin α-KTx 7.1, Pandinotoxin-α, Potassium channel-blocking toxin 2, Pi-2, Pi2, Toxin PiTX-K-α, PiTX-Kα
A Blocker of A-Type and Shaker-Related Voltage-Gated K+ Channels
Cat #: STP-500
Alternative Name Potassium channel toxin α-KTx 7.1, Pandinotoxin-α, Potassium channel-blocking toxin 2, Pi-2, Pi2, Toxin PiTX-K-α, PiTX-Kα
Lyophilized Powder yes
  • Bioassay Tested
  • Origin Synthetic peptide
    MW: 4033 Da.
    Purity: >98% (HPLC)
    Effective concentration 10-200 nM.
    Sequence TISCTNPKQCYPHCKKETGYPNAKCMNRKCKCFGR.
    Modifications Disulfide bonds between Cys4-Cys25, Cys10-Cys30, Cys14-Cys32.
    Structure
    Molecular formula C169H267N53O48S7.
    CAS No.: 185529-64-0.
    Activity Pandinotoxin Kα is an A-type and Shaker-related K+ channel blocker1-4.
    References-Activity
    1. Gomez-Lagunas, F. et al. (1996) J. Memb. Biol. 152, 49.
    2. Tenenholz, T.C. et al. (1997) Biochemistry 36, 2763.
    3. Rogowski, R.S. et al. (1996) Mol. Pharmacol. 50, 1167.
    4. Whyment, A.D. et al. (2011) Neuroscience 178, 68.
    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 other 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 Pandinotoxin Kα inhibits KV1.2 channels heterologously expressed in Xenopus oocytes.
      Alomone Labs Pandinotoxin Kα inhibits KV1.2 channels heterologously expressed in Xenopus oocytes.
      A. Time course of Pandinotoxin Kα (#STP-500) action on KV1.2 currents.  KV1.2 currents were elicited by 100 ms voltage ramp from the holding potential of -80 mV to +10 mV. 10 nM and 100 nM Pandinotoxin Kα were perfused as indicated by the bars at -10 mV. B. Superimposed examples of KV1.2 channel current in the absence (control) and presence of 10 nM or 100 nM Pandinotoxin Kα (taken from the experiment in A).
    References - Scientific background
    1. Aiyar, J. et al. (1996) J. Biol. Chem. 271, 31013.
    2. Tenenholz, T.C. et al. (1997) Biochemistry 36, 2763.
    3. Goldstein, S.A. et al. (1994) Neuron 12, 1377.
    4. MacKinnon, R. et al. (1988) Neuron 1, 997.
    Scientific background

    Scorpion venoms are a rich source of ion channel modulators. The scorpion toxins have been useful molecules in probing the K+ channel structures and functions1.

    Pandinotoxin Kα (PiTx-Kα) is a 35 amino acid peptidyl toxin isolated from the Pandinus imperator (Emperor scorpion) venom. It is a highly potent and selective blocker of voltage-activated K+ channels. PiTx-Kα preferentially blocks rapidly inactivating (A-type) K+ channels2. In general, channel inhibitors can be pore blockers or gating modifiers. Pore blockers bind to the channel in 1:1 stoichiometry and plug the pore of the channel impeding the flow of the ionic current. These toxins are small proteins that block the passage of K+ ions by binding at the pore entryway on the extracellular side of the channel, thereby inhibiting the ion flux3. The interactions of toxins with K+ channels are among the strongest and most specific known in protein-protein complexes4.

    Target A-type and Shaker-related K+ channels
    Net Peptide Content: 100%
    Last update: 23/08/2020

    Pandinotoxin Kα (#STP-500) is a highly pure, synthetic, and biologically active peptide toxin.

    For research purposes only, not for human use
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