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HsTx1 Toxin

Potassium channel toxin α-KTx 6.3, Neurotoxin HsTX1

A Potent Blocker of KV1.3 K+ Channels

Cat #: STH-300
Alternative Name Potassium channel toxin α-KTx 6.3, Neurotoxin HsTX1
Lyophilized Powder yes
  • Bioassay Tested
  • Origin Synthetic peptide
    MW: 3819 Da
    Purity: >99% (HPLC)
    Form Lyophilized powder.
    Effective concentration 1-100 pM.
    Modifications Disulfide bonds between Cys3-Cys24, Cys9-Cys29, Cys13-Cys31 and Cys19-Cys34 . Cys34-C-terminal amidation.
    Molecular formula C149H246N54O46S9.
    Activity HsTx1 Toxin is a highly potent KV1.3 blocker1.
    1. Lebrun, B. et al.  (1997) Biochem. J. 328, 321.
    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 HsTx-1 Toxin inhibits KV1.3 channels heterologously expressed in Xenopus oocytes. 
      Alomone Labs HsTx-1 Toxin inhibits KV1.3 channels heterologously expressed in Xenopus oocytes. 
      A. Time course of HsTx1 Toxin (#STH-300) action on KV1.3 currents. Current amplitudes were plotted as a function of time. Membrane potential was held at -80 mV and oocytes were stimulated by a 100 ms voltage ramp to +10 mV. 0.5 nM HsTx1 Toxin was perfused during 160 sec, as indicated (green) at 0 mV (70% inhibition) and -12 mV (95% inhibition). B. Superimposed examples of KV1.3 channel current in the absence (black) and presence (green) of 0.5 nM HsTx1 Toxin (taken from the experiment in A).
    References - Scientific background
    1. Miller, C.  et al. (1995) Neuron 15, 5.
    2. Bontems, F.  et al. (1991) Science 254, 1521.
    3. Martinez, F. et al. (1998) FEBS Lett 429, 381.
    4. Lebrun, B. et al.  (1997) Biochem. J. 328, 321.
    5. Kharrat, R. et al. (1996) Eur. J. Biochem242, 491.
    Scientific background

    Many K+ channel blockers have been identified in the scorpion venom1. These peptide toxins consist of 29 to 39 amino acids, and commonly share three disulfide bonds. Their 3D structure comprises a helix and a double- or triple-stranded β-sheet2. The functional sites of the toxins are located either on the solvent exposed face of the β-sheet, or on the helix, depending on the type of K+ channel targeted3.

    Potassium channel toxin alpha-KTx 6.3 (HsTx1) is a 34 amino acid peptidyl toxin isolated from the Heterometrus spinifer (Asia giant forest scorpion, Malaysian black scorpion) venom4. HsTx1 is one of the most active peptidic inhibitors of rat KV1.3 channels ever described, with an IC50 of approx. 12 pM4. HsTX1 belongs to a structural class of scorpion K+ channel inhibitors which includes Pandinus imperator toxin 1 (Pi1) and Maurotoxin (MTX) (#STM-340), two toxins containing 35 residues and four disulphide bridges5.

    Target KV1.3 K+ channels
    Peptide Content: 100%
    Last update: 06/11/2022

    HsTx1 Toxin (#STH-300) is a highly pure, synthetic, and biologically active peptide toxin.

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