High conductance Ca2+-activated K+ channel blocker. Highly selective for Kv1.1 and Kv1.3. Blocking of Kv1.3 inhibits T cell activation.
Product Specification
| Alternative Name: | KTx |
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| Sequence: | H-Gly-Val-Glu-Ile-Asn-Val-Lys-Cys-Ser-Gly-Ser-Pro-Gln-Cys-Leu-Lys-Pro-Cys-Lys-Asp-Ala-Gly-Met-Arg-Phe-Gly-Lys-Cys-Met-Asn-Arg-Lys-Cys-His-Cys-Thr-Pro-Lys-OH
(Disulfide bonds between Cys8-Cys28, Cys14-Cys33 and Cys18-Cys35) |
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| Formula: | C171H283N55O49S8 |
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| MW: | 4150.0 |
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| Source: | Synthetic. Originally isolated from Androctonus mauretanicus mauretanicus scorpion venom. |
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| CAS: | 145199-73-1 |
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| Purity: | ≥98% |
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| Appearance: | Lyophilized. |
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| Solubility: | Soluble in water. |
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| Shipping: | Ambient |
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| Long Term Storage: | -20°C |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR: A. Lange, et al.; Nature
440, 959 (2006),
Abstract;
Selective blockade of voltage-gated potassium channels reduces inflammatory bone resorption in experimental periodontal disease: P. Valverde, et al.; J. Bone Miner. Res.
19, 955 (2004),
Abstract;
Selective blocking of voltage-gated K+ channels improves experimental autoimmune encephalomyelitis and inhibits T cell activation: C. Beeton, et al.; J. Immunol.
166, 936 (2001),
Abstract;
Distribution in rat brain of binding sites of kaliotoxin, a blocker of Kv1.1 and Kv1.3 alpha-subunits: C. Mourre, et al.; J. Pharmacol. Exp. Ther.
291, 943 (1999),
Abstract;
3D structure of kaliotoxin: is residue 34 a key for channel selectivity?: M. Gairi, et al.; J. Pept. Sci.
3, 314 (1997),
Abstract;
Synthesis and characterization of kaliotoxin. Is the 26-32 sequence essential for potassium channel recognition?: R. Romi, et al.; J. Biol. Chem.
268, 26302 (1993),
Abstract;
Full Text
Kaliotoxin, a novel peptidyl inhibitor of neuronal BK-type Ca(2+)- activated K+ channels characterized from Androctonus mauretanicus mauretanicus venom: M. Crest, et al.; J. Biol. Chem.
267, 1640 (1992),
Abstract;
Full Text
