Charybdotoxin
Pharmacological properties
Charybdotoxin is a 37 amino acid peptide isolated from the venom of the scorpion Leiurus quinquestriatus hebraeus that blocks voltage gated and Ca2+ activated K+ channels. This blockade causes hyperexcitability of the nervous system. The toxin reversibly blocks channel activity by interacting at the external pore of the channel protein with an apparent Kd of 2.1 nM. ChTX also blocks Kv1.2 (Kd 14 nM) and Kv1.3 (Kd 2.6nM) channels.
Product specifications
AA sequence: H-Pyr-Phe-Thr-Asn-Val-Ser-Cys7-Thr-Thr-Ser-Lys-Glu-Cys13-Trp-Ser-Val-Cys17-Gln-Arg-Leu-His-Asn-Thr-Ser-Arg-Gly-Lys-Cys28-Met-Asn-Lys-Lys-Cys33-Arg-Cys35-Tyr-Ser-OH
(Disulfide bonds between Cys7-Cys28, Cys13-Cys33, and Cys17-Cys35)
Length (aa): 37
Formula: C176H277N57O55S7
Molecular Weight: 4295.90 Da
Appearance: White lyophilized solid
Solubility: water and saline buffer
CAS number: 95751-30-7
Source: Synthetic
Purity rate: > 97%
Price & quantities
- 50 µg: 100 €
- 5 x 50 µg: 400 €
- 100 µg: 170 €
- 500 µg: 425 €
Other quantities available upon request
Related products
| Maurotoxin | Apamin | Leiurotoxin 1 | Tamapin |
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References
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Gimenez-Gallego G., et al. (1988) Purification, sequence, and model structure of charybdotoxin, a potent selective inhibitor of calcium-activated potassium channels. Proc. Natl. Acad. Sci. U.S.A. 85:3329-3333. PubMed link
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Goldstein SA, Miller C. (1993) Mechanism of charybdotoxin block of a voltage-gated K+ channel. Biophys J. 65(4):1613-9. PubMed link
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Goldstein SA, Pheasant DJ, Miller C. (1994) The charybdotoxin receptor of a Shaker K+ channel: peptide and channel residues mediating molecular recognition. Neuron. 12(6):1377-88. PubMed link