Potent blocker of potassium channels

Kaliotoxin-1 (KTX1) has been isolated from the venom of the Scorpion Androctonus mauretanicus mauretanicus. Kaliotoxin-1 shows a high structural affinity with Iberiotoxin and Charybdotoxin that inhibit KCa2+ channels activity. According to several studies, it appears that Kaliotoxin-1 has a weak inhibitory effect on KCa2+ channels, but it is a potent and selective inhibitor of voltage-activated potassium channel (Kv1.1, Kv1.2, Kv1.3).

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AA sequence: Gly-Val-Glu-Ile-Asn-Val-Lys-Cys8-Ser-Gly-Ser-Pro-Gln-Cys14-Leu-Lys-Pro-Cys18-Lys-Asp-Ala-Gly-Met-Arg-Phe-Gly-Lys-Cys28-Met-Asn-Arg-Lys-Cys33-His-Cys35-Thr-Pro-Lys-OH
(Disulfide bonds between Cys8-Cys28, Cys14-Cys33 and Cys18-Cys35)
Length (aa): 38
Formula: C171H283N55O49S6
Molecular Weight: 4149.89 Da
Appearance: White lyophilized solid
Solubility: water and saline buffer
CAS number:
Source: Synthetic
Purity rate: > 97 %









Neuropathophysiological effect and immuno-inflammatory response induced by kaliotoxin of androctonus scorpion venom

Heterogeneous competition of Kv1 channel toxins with kaliotoxin for binding in rat brain: autoradiographic analysis

Kaliotoxin, a Kv1.1 and Kv1.3 channel blocker, improves associative learning in rats

Selective blocking of voltage-gated K+ channels improves experimental autoimmune encephalomyelitis and inhibits T cell activation

Distribution in rat brain of binding sites of kaliotoxin, a blocker of Kv1.1 and Kv1.3 alpha-subunits

3D structure of kaliotoxin: is residue 34 a key for channel selectivity?

T cell activation is regulated by voltage-dependent and calcium-activated potassium channels

Effects of channel modulators on cloned large-conductance calcium-activated potassium channels

Pharmacological properties of Ca2+activated K+ currents of ramified murine brain macrophages

Kaliotoxin, a novel peptidyl inhibitor of neuronal BK-type Ca(2+)-activated K+ channels characterized from Androctonus mauretanicus mauretanicus venom