1Kβ-Pompilidotoxin

1Kβ-PMTX
An Activator of NaV Channels
    Cat #: P-182
    Alternative Name 1Kβ-PMTX
  • Lyophilized Powder
  • Bioassay Tested
  • Origin Synthetic peptide
    MW: 1531 Da.
    Purity: >98% (HPLC)
    Effective concentration 100-200 µM.
    Sequence KIKIGLFDQLSRL.
    Modifications Leu13 – C-terminal amidation.
    Structure
    • 1Kβ-Pompilidotoxin
    Molecular formula C71H124N20O17.
    Activity 1Kβ-PMTX slows NaV channel inactivation without changing the peak current-voltage relationship or the activation time course of the TTX-sensitive Na+ currents in the neuromuscular synapse1-3. 1Kβ-PMTX showed the largest effects on the various tested NaV isoforms, mainly on NaV1.6 channels1.
    References-Activity
    1. Schiavon, E. et al. (2010) FEBS J. 277, 918.
    2. Sahara, Y. et al. (2000) Eur. J. Neurosci. 12, 1961.
    3. Konno, K. et al. (2000) Neurosci. Lett. 285, 29.
    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, pH > 8. 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
    • 1Kβ-Pompilidotoxin
      Alomone Labs 1Kβ-Pompilidotoxin enhances native NaV currents in ND7-23 cells.
      Native TTX-sensitive NaV currents in ND7-23 cells were elicited by a 50 ms voltage ramp from the holding potential of -100 mV to +60 mV, applied every 10 sec using whole-cell voltage clamp. A. Time course, showing the effect of 200 µM 1Kβ-Pompilidotoxin (#P-182) application (horizontal bar) on current area, indicative of a toxin-dependent decrease in NaV currents inactivation. B. Superimposed traces of NaV currents in ND7-23 cells under control conditions and after 2 min perfusion with 200 µM 1Kβ-PMTX (as indicated).
    • 1Kβ-Pompilidotoxin
      Alomone Labs 1Kβ-Pompilidotoxin enhances NaV1.6 currents heterologously expressed in Xenopus oocytes.
      NaV1.6 currents were elicited by a 100 ms voltage step from a holding potential of -100 mV to 0 mV applied every 10 sec, using two electrode voltage clamp. A. Time course, showing the effect of 20 µM, 50 µM and 100 µM 1Κβ-Pompilidotoxin (#P-182) application (horizontal bars) on current area. B. Superimposed traces of NaV1.6 current under control conditions and after 2 min perfusion with 20 µM, 50 µM and 100 µM 1Κβ-Pompilidotoxin (as indicated).
    References - Scientific background
    1. Schiavon, E. et al. (2010) FEBS J. 277, 918.
    2. Sahara, Y. et al. (2000) Eur. J. Neurosci. 12, 1961.
    3. Konno, K. et al. (2000) Neurosci. Lett. 285, 29.
    4. Konno, K. et al. (1998) Biochem. Biophys. Res. Commun. 250, 612.
    5. Harsch, A. et al. (1998) Neurosci. Lett. 252, 49.
    Scientific background

    1Kβ-PMTX is a mutated form of the β-PMTX (#P-180), originally isolated from the solitary wasp (Batozonellus maculifrons) venom and is a synthetic version of the peptide1. Pompilidotoxins (PMTX, α and β) are small peptides consisting of 13 amino acids.

    β-PMTX induces a unique pattern of repetitive action potentials previous seen with other neurotoxins and thus facilitates both excitatory and inhibitory synaptic transmission.

    Recently it was found that this toxin slows the Na+-channel inactivation, without changing the peak current-voltage relationship or the activation time course of the TTX-sensitive Na+ currents in the neuromuscular synapse of the lobster walking leg and in the rat trigeminal ganglion neurons2-4. It is effective at concentrations of 10 nM in cultured rat cortical neurons5.

    1Kβ-PMTX is mutated at position 1 with Arginine to Lysine transition, which enhances its activity on voltage-gated human Nav1.6 Na+ channels relative to native β-PMTX1,3.

    Target NaV Na+ channels
    Net Peptide Content: 100%
    Last update: 24/01/2020

    1Kβ-Pompilidotoxin (#P-182) is a highly pure, synthetic, and biologically active peptide toxin.

    For research purposes only, not for human use
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