Agitoxin-3

K+ channel toxin α-KTx 3.3, AgTx-3, AgTx3
A Potent Blocker of KV1.3 K+ Channels
    Cat #: STA-390
    Alternative Name K+ channel toxin α-KTx 3.3, AgTx-3, AgTx3
  • Lyophilized Powder
  • Bioassay Tested
  • Origin Synthetic peptide
    MW: 4101 Da.
    Purity: >98% (HPLC)
    Form Lyophilized
    Effective concentration 50 pM - 10 nM.
    Sequence GVPINVPCTGSPQCIKPCKDAGMRFGKCMNRKCHCTPK.
    Modifications Disulfide bonds between Cys8-Cys28, Cys14-Cys33, and Cys18-Cys35.
    Structure
    • Agitoxin-3
    Molecular formula C171H280N54O47S8
    CAS No.: 155646-23-4
    Activity Agitoxin-3 is a blocker of Shaker voltage-gated K+ channels as well as the mammalian homologues of Shaker.
    References-Activity
    1. Garcia, M.L. et al. (1994) Biochemistry 33, 6834.
    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
    • Agitoxin-3
      Alomone Labs Agitoxin-3 blocks KV1.3 channels expressed in Xenopus oocytes.
      A. Representative time course of KV1.3 current inhibition by Agitoxin-3 (#STA-390). Membrane potential is held at -100 mV. Current elicited by a 100 ms voltage ramp to +60 mV every 10 sec is significantly inhibited by 0.5 nM Agitoxin-3 (green). B. Superimposed traces of KV1.3 current before (black) and after application of 0.5 nM Agitoxin-3 (green), 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 K+ channels
    Net Peptide Content: 100%
    Last update: 03/03/2020

    Agitoxin-3 (#STA-390) is a highly pure, recombinant, and biologically active peptide toxin.

    For research purposes only, not for human use

    Applications

    Specifications

    Scientific Background

    Citations

    Citations
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