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Charybdotoxin

(HB1052)
Data

Product overview

  • Name
    Charybdotoxin
  • Short description
    Potent, selective KCa channel inhibitor
  • Biological description
    Potent and selective KCa channel inhibitor (Kd = 3.5 nM). Displays high affinity for Kv1.3. Also a homotetrameric F425H channel blocker (Kd = 48 nM). Found in venom of the Leiurus quinquestriatus hebraeus scorpion.
  • Alternative names
    ChTx
  • Biological action
    Inhibitor
  • Citations

Properties

  • Molecular Weight
    4295.95
  • Molecular Formula
    C176H277N57O55S7
  • CAS Number
    95751-30-7
  • PubChem identifier
    102594130
  • SMILES
    [H]N1[C@@H](CCC1=O)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CO)C(=O)N[C@H]1CSSC[C@@H]2NC(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC3=CNC=N3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H]3CSSC[C@H](NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CSSC[C@H](NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@@H](NC1=O)[C@@H](C)O)[C@@H](C)O)C(=O)N[C@@H](CC1=CNC4=C1C=CC=C4)C(=O)N[C@@H](CO)C(=O)N[C@@H](C(C)C)C(=O)N3)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCSC)NC2=O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CO)C(O)=O)[C@@H](C)O
  • InChiKey
    CNVQLPPZGABUCM-UHFFFAOYSA-N

Storing and Using Your Product

  • Storage instructions
    -20°C (desiccate)
  • Solubility overview
    soluble in water (1mg/ml)
  • Important
    This product is for RESEARCH USE ONLY and is not intended for therapeutic or diagnostic use. Not for human or veterinary use.

References for Charybdotoxin

  • Purification, sequence, and model structure of charybdotoxin, a potent selective inhibitor of calcium-activated potassium channels.

    Gimenez-Gallego G et al (1988) Proc Natl Acad Sci U S A 85(10) : 3329-33.
    PubMedID: 2453055
  • Interaction of agitoxin2, charybdotoxin, and iberiotoxin with potassium channels: selectivity between voltage-gated and Maxi-K channels.

    Gao YD et al (2003) Proteins 52(2) : 146-54.
    PubMedID: 12833539
  • Electrostatic interaction between charybdotoxin and a tetrameric mutant of Shaker K(+) channels.

    Thompson J et al (2000) Biophys J 78(5) : 2382-91.
    PubMedID: 10777734
  • Charybdotoxin and margatoxin acting on the human voltage-gated potassium channel hKv1.3 and its H399N mutant: an experimental and computational comparison.

    Nikouee A et al (2012) J Phys Chem B 116(17) : 5132-40.
    PubMedID: 22490327
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