µ/κ-Theraphotoxin-Hl2a, µ/κ-TRTX-Hl2a, Peptide D

A Blocker of NaV1.3 Na+ Channel and HERG K+ Channel

Cat #: STT-200
Alternative Name µ/κ-Theraphotoxin-Hl2a, µ/κ-TRTX-Hl2a, Peptide D
Lyophilized Powder yes
  • Bioassay Tested
  • Origin Synthetic peptide
    MW: 3708 Da
    Purity: >98% (HPLC)
    Effective concentration 100-500 nM.
    Modifications Disulfide bonds between Cys2-Cys17, Cys9-Cys22, Cys16-Cys29. IIe33 – C-terminal amidation.
    • This product is sold under license from Alomone Preclinical Ltd.
    Molecular formula C161H248N46O43S6.
    Activity Haplotoxin-2 inhibits voltage-gated Na+ channels NaV1.3 as well as KV11.1 (hERG) channels1.
    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.
    Our bioassay
    • Alomone Labs Haplotoxin-2 inhibits rNaV1.3 and hERG channels heterologously expressed in HEK293 cells.
      Alomone Labs Haplotoxin-2 inhibits rNaV1.3 and hERG channels heterologously expressed in HEK293 cells.
      A. Dose-response of NaV and KV channels inhibition by Haplotoxin-2 (#STT-200). 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 human KV11.1 (hERG) expressed in HEK293 cells (open triangles). B. Example of superimposed current traces of rat NaV1.3 channel activity before and during application of 0.15 µM of Haplotoxin-2. 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.
    References - Scientific background
    1. Meir, A et al. (2011). Novel peptides isolated from spider venom, and uses thereof. U.S. Patent Application Publication # US 2011/0065647 A1.
    2. Sheets, P.L. et al. (2008) J. Pharmacol. Exp. Ther. 326, 89.
    3. Zimmermann, K. et al. (2007) Nature 447, 855.
    4. Amir, E. et al. (2006) J. Pain 7, S1.
    Scientific background

    Haplotoxin-2 is isolated from the Haplopelma Lividum spider venom and is a synthetic version of the peptide1.

    Haplotoxin-2 inhibits voltage-gated rat NaV1.3 Na+ channels.

    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 therapeutics2-3.

    The expression and functional properties of NaV channels in peripheral sensory neurons can be dynamically regulated following axonal injury or peripheral inflammation4.

    Haplotoxin-2 shows high homology to Huwentoxin-I (78%), Hainantoxin-III (#STH-120) (76%) and Phrixotoxin-3 (#STP-720) (65%).

    Target NaV1.3 Na+ channels, KV11.1 K+ channels
    Peptide Content: 100%
    Last update: 06/11/2022

    Haplotoxin-2 (#STT-200) is a highly pure, synthetic, and biologically active peptide toxin.

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