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Cn2 Toxin

Toxin 2, Toxin II.9.2.2, β-mammal toxin Cn2

An activator of Nav1.6

Cat #: STC-060
Alternative Name Toxin 2, Toxin II.9.2.2, β-mammal toxin Cn2
Lyophilized Powder yes
  • Bioassay Tested
  • Origin Centruroides noxius (Mexican scorpion)
    Source Synthetic
    MW: 7589 Da
    Purity: >98%
    Form Lyophilized powder
    Effective concentration 0.02-0.5 µM
    Sequence KEGYLVDKNTGCKYECLKLGDNDYCLRECKQQYGKGAGGYCYAFACWCTHLYEQAIVWPLPNKRCS-NH2
    Modifications Disulfide bonds between: Cys12-Cys65, Cys16-Cys41, Cys25-Cys46, Cys29-Cys48
    Ser66 - amidation
    Structure
    Molecular formula C336H495N89O97S8
    Activity Cn2 toxin simultaneously induces both the left shift voltage-dependent activation and a transient resurgent current only in human Nav1.6 channels. Cn2 also produced both actions in mouse cerebellar Purkinje neurons and blocked firing at appropriate concentrations1.
    References-Activity
    1. Schiavon, E. et al. (2006) J. Biol. Chem. 281, 20326.
    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 Soluble in DDW.
    Centrifuge all products before use (10000 x g 5 min).
    Storage of solutions Store at 4°C for up to 1 week. For longer periods, small aliquots should be stored at -20°C. Avoid multiple freezing and thawing.
    Our bioassay
    • Alomone Labs Cn2 Toxin activates Nav1.6 channels expressed in Xenopus oocytes.

      Alomone Labs Cn2 Toxin activates Nav1.6 channels expressed in Xenopus oocytes.
      A. Representative traces of Nav1.6 channel currents before and after application of 100 nM (magenta) and 500 nM (green) Cn2 Toxin (#STC-060). Cn2 Toxin caused a significant current at a voltage that does not normally activate the channels. A double protocol with an initial holding potential of -120 mV was conditioned by a prepulse of +35 mV for 20 ms, while the second pulse to -40 mV for 50 ms was preceded by 30 ms at -100 mV.
      B. Representative time course of current amplitude at -40 mV before, during application of 100 nM and 500 nM Cn2 Toxin (indicated by bars) and upon wash, demonstrating the current amplitude enhancement.
    References - Scientific background
    1. Chen, R. and Chung, S.H. (2012) J. Phys. Chem. 16, 4796.
    2. Schiavon, E. et al. (2006) J. Biol. Chem. 281, 20326.
    3. Israel, M.R. et al. (2019) J. Physiol. 597.14, 3751.
    4. Escalona, M.P. et al. (2014) J. Proteomics 111, 212.
    5. Pintar, A. et al. (1999) J. Mol. Biol. 2, 359.
    6. Israel, M.R. et al. (2018) J. Med. Chem. 61, 1730.
    Scientific background

    Cn2 Toxin is a β-scorpion toxin, isolated from the venom of Centruroides noxius, a Mexican native scorpion species. It belongs to the scorpion β-toxins family that bind to the voltage-sensing domain of voltage-gated sodium (NaV) channels and trap the voltage-sensing domain in the activated state1.  This unique toxin is capable of simultaneously inducing both the left shift voltage-dependent activation and a transient resurgent current only in human NaV1.6 channels, among the other TTX-sensitive isoforms2. Cn2 also produced both actions in mouse cerebellar Purkinje neurons and blocked firing at appropriate concentrations2.

    NaV1.6 plays an essential role in peripheral sensory neurons, specifically at the distal terminals of mechanosensing fibers innervating the skin and colon. NaV1.6 activation by Cn2 Toxin leads to enhanced response to mechanical stimulus in vivo3. Cn2 Toxin facilitates Nav1.6 early channel opening, and increased persistent and resurgent currents in large-diameter DRG neurons in a unique mechanism of action3.

    Cn2 Toxin was described also as a modifier of the neuronal structure and induces apoptosis and reduction of the proliferation and cell survival in experiments performed in F11 mouse neuroblastoma cells4.

    The crystal structure of this toxin was determined and it was shown to be a 66 amino acid polypeptide that shares a similar structure with other scorpion toxins acting on sodium channels. It is made of a triple-stranded antiparallel β-sheet and an α-helix, and is stabilized by four disulfide bridges. It contains a hydrophobic core, a hydrophobic patch and a positively charged patch5,6.

    Target Nav1.6 channels
    Net Peptide Content: 100%

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    Last update: 24/01/2021

    Cn2 Toxin (#STC-060) is a highly pure, synthetic and biologically active toxin.

    For research purposes only, not for human use

    Applications

    Specifications

    Scientific Background

    Citations

    Citations
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