VSTX3

κ-Theraphotoxin-Gr4a, Kappa-TRTX-Gr4a, Voltage sensor toxin 3, Peptide F
A Blocker of NaV1.3, NaV1.7, NaV1.8 Voltage-Gated Na+ Channels
    Cat #: STT-350
    Alternative Name κ-Theraphotoxin-Gr4a, Kappa-TRTX-Gr4a, Voltage sensor toxin 3, Peptide F
  • Lyophilized Powder
  • Bioassay Tested
  • Origin Synthetic peptide
    MW: 4172 Da.
    Purity: >98% (HPLC)
    Effective concentration 200-500 nM.
    Sequence DCLGWFKGCDPDNDKCCEGYKCNRRDKWCKYKLW.
    Modifications Disulfide bonds between Cys2-Cys17, Cys9-Cys22, Cys16-Cys29.
      • This product is sold under license from Alomone Preclinical Ltd.
        VSTX3
    Molecular formula C182H261N51O51S6.
    Activity VSTX3 inhibits voltage-gated Na+ channels NaV1.3, NaV1.7 and NaV1.81.
      • Meir, A. et al. (2011) Novel peptides isolated from spider venom, and uses thereof. U.S. Patent Application Publication # US 2011/0065647 A1.
    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 20 mM ammonium acetate or 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.
      • VSTX3
        Alomone Labs VSTX3 inhibits rNaV1.3 and rNaV1.8 channels heterologously expressed in HEK293 and  ND7-23 cells, respectively.
        A. Dose-response of NaV channels inhibition by VSTX3 (#STT-350). The inhibition was measured in 3-5 cells for each dose in rat NaV1.3 channels expressed in HEK293 cells (open circles) and 3-5 cells for rat NaV1.8 expressed in ND7-23 cells (open square) in the presence of 600 nM Tetrodotoxin citrate (#T-550). B. Example of superimposed current traces of rat NaV1.3 channel activity before (black) and during (green) application of 0.1 µM VSTX3. Holding potential was -100 mV and currents were stimulated every 10 seconds by a voltage ramp of 40 msec from holding potential to +60 mV. C. Example of superimposed current traces of rat NaV1.8 channel activity before (black) and during (green) application of 0.5 µM VSTX3, both in the presence of 600 nM Tetrodotoxin (with citrate). The same voltage protocol was used as in graph B.
    References - Scientific background
    • 1. Ruta, V. and MacKinnon, R. (2004) Biochemistry 43, 10071.
    • 2. Meir, A. et al. (2011) Novel peptides isolated from spider venom, and uses thereof. U.S. Patent Application Publication # US 2011/0065647 A1.
    • 3. Sheets, P.L. et al. (2008) J. Pharmacol. Exp. Ther. 326, 89.
    • 4. Zimmermann, K. et al. (2007) Nature 447, 855.
    • 5. Amir, E. et al. (2006) J. Pain 7, S1.
      • VSTX3 was originally isolated from the Grammostola spatulata spider venom1 and is also isolated from the Phrixotrichus auratus spider venom2.

        VSTX3 was first isolated and shown to bind through its affinity to the voltage-sensor domain of KvAP channels1.

        VSTX3 also inhibits voltage-gated rat NaV1.3, NaV1.7 and NaV1.8 Na+ channels2.

        Voltage-gated sodium channels (VGSC, NaV) play a critical role in excitability of nociceptors (pain-sensing neurons). The peripheral-specific sodium channels NaV1.7, NaV1.8 and NaV1.9 are particularly important in the pathophysiology of different pain syndromes and hence, thought to be potential targets for pain therapeutics3,4.

        The expression and functional properties of NaV channels in peripheral sensory neurons can be dynamically regulated following axonal injury or peripheral inflammation5.

        VSTX3 shows high homology to Ceratotoxin-1 (75%), Ceratotoxin-2 (#STC-100) (77%) and Pterinotoxin-1 (#STT-100) (83%).

    Target NaV1.3, NaV1.7, NaV1.8 Na+ channels
    Net Peptide Content: 100%
    Last update: 15/10/2019

    VSTX3 (#STT-350) is a highly pure, synthetic, and biologically active peptide toxin.

    For research purposes only, not for human use