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K+ channel toxin α-KTx 3.4, Leiurotoxin-2, AgTx-1, AgTx1, Leiurotoxin II, LeTx II

A Potent Blocker of KV1.3 Channels

Cat #: STA-150
Alternative Name K+ channel toxin α-KTx 3.4, Leiurotoxin-2, AgTx-1, AgTx1, Leiurotoxin II, LeTx II
Lyophilized Powder yes
  • Bioassay Tested
  • Origin Synthetic peptide
    MW: 4015 Da
    Purity: >98% (HPLC)
    Effective concentration <1 nM.
    Modifications Disulfide bonds between Cys8-Cys28, Cys14-Cys33, and Cys18-Cys35.
    Molecular formula C169H278N52O47S7.
    CAS No.: 155646-21-2
    Activity Agitoxin-1 is a blocker of Shaker voltage-gated K+ channels as well as the mammalian homologues of Shaker.
    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 aqueous buffer. Centrifuge all product preparations before use (10000 x g 5 min).
    Storage of solutions Up to one week at 4°C or three months at -20°C.
    Our bioassay
    • Alomone Labs Agitoxin-1 blocks KV1.3 channels expressed in Xenopus oocytes.
      Alomone Labs Agitoxin-1 blocks KV1.3 channels expressed in Xenopus oocytes.
      A. Representative time course of Agitoxin-1 (#STA-150) inhibition of KV1.3 current. Membrane potential was held at -100 mV. Current elicited by a 100 ms voltage ramp to +60 mV every 10 sec was significantly and reversibly inhibited by 2 min applications of 0.5 nM and 5 nM Agitoxin-1, as indicated. B. Superimposed traces of KV1.3 current before and after application of 0.5 nM and 5 nM Agitoxin-1, taken from the recording in A.
    References - Scientific background
    1. Bergeron, Z.L. and Bingham, J.P. (2012) Toxins 4, 1082.
    2. Garcia, M.L. et al. (1994) Biochemistry 33, 6834.
    3. Aggarwal, S.K. and MacKinnon, R. (1996) Neuron 6, 1169.
    Scientific background

    Agitoxins are peptide toxins originally isolated from L. quinquestriatus hebraeus scorpion venom. This group of toxins blocks potassium (K⁺) channels and has a central role in the investigation and understanding of the physiological importance of K+ channels and their function in membrane biophysics1.

    Agitoxins 1, 2 and 3 have been isolated and characterized. Each toxin is comprised of 38 amino acids. They are highly homologous and differ only in the identity of the residues at positions 7, 15, 29 and 31.

    Agitoxins appear to be specific for the Shaker K+ channel of Drosophila melanogaster and many of the mammalian homologues of Shaker. Agitoxin-1 blocks the Shaker channel in a stoichiometry of one to one, it binds the channel site in the extracellular vestibule and prevents ion conduction by occluding the pore2.

    Using scorpion toxins for molecular dissection of ion channels has led to direct evidence that specific mutations can be correlated to changes in the propagation and conduction of electrical impulses in the body3.

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

    Agitoxin-1 (#STA-150) is a highly pure, synthetic, and biologically active peptide toxin.

    For research purposes only, not for human use



    Product citations
    1. Meneses, D. et al. (2016) Neural Plast. 2016, 8782518.
    2. Druzin, M. et al. (2011) PLoS ONE 6, e20213.
    3. Al-Sabi, A. et al. (2010) J. Gen. Physiol. 136, 273.


    Scientific Background

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