Replaces Prod. #: BML-KC100
A potent and selective inhibitor of the high conductance Ca2+-activated K+ channel. It inhibits K+ conductance and mitogen-stimulated proliferation (Ki=300 and 500pM, respectively) in human T lymphocytes. Does not affect apamin-sensitive channels.
Product Details
| Alternative Name: | ChTx |
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| Sequence: | Pyr-Phe-Thr-Asn-Val-Ser-Cys-Thr-Thr-Ser-Lys-Glu-Cys-Trp-Ser-Val-Cys-Gln-Arg-Leu-His-Asn-Thr-Ser-Arg-Gly-Lys-Cys-Met-Asn-Lys-Lys-Cys-Arg-Cys-Tyr-Ser-OH(Disulfide bonds between Cys7-Cys28, Cys13-Cys33 and Cys17-Cys35) |
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| Formula: | C176H277N57O55S7 |
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| MW: | 4295.9 |
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| Source: | Synthetic. |
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| CAS: | 95751-30-7 |
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| MI: | 14: 2046 |
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| Formulation: | Lyophilized. |
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| Reconstitution: | Do not remove cap. Inject distilled water into the vial using a calibrated syringe. Dissolve all contents thoroughly to receive a 0.1mM solution. Prepare aliquots (100-200µl) and store at -20°C. The aqueous solution should be used within a few weeks. |
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| Shipping: | Ambient Temperature |
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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
Opening of small and intermediate calcium-activated potassium channels induce relaxation mainly mediated by NO release in large arteries and EDHF in small arteries from rat: E. Stankevicius, et al.; J. Pharmacol. Exp. Ther.
339, 842 (2011),
Abstract;
Full Text
The GPR55 agonist lysophosphatidylinositol directly activates intermediate-conductance Ca2+ -activated K+ channels: A.I. Bondarenko, et al.; Pflugers Arch.
462, 245 (2011),
Abstract;
Full Text
Block of maurotoxin and charybdotoxin on human intermediate-conductance calcium-activated potassium channels (hIKCa1): V. Visan, et al.; Toxicon
43, 973 (2004),
Abstract;
Interaction of agitoxin2, charybdotoxin, and iberiotoxin with potassium channels: selectivity between voltage-gated and Maxi-K channels: Y. D. Gao & M. L. Garcia; Proteins
52, 146 (2003),
Abstract;
A charybdotoxin-insensitive conductance in human T lymphocytes: T cell membrane potential is set by distinct K+ channels: J. A. Verheugen & H. Korn; J. Physiol.
503, 317 (1997),
Abstract;
Effects of charybdotoxin on K+ channel (KV1.2) deactivation and inactivation kinetics: L.K. Sprunger, et al.; Eur. J. Pharmacol.
314, 357 (1996),
Abstract;
Charybdotoxin and its effects on potassium channels: M.L. Garcia, et al.; Am. J. Physiol.
269, C1 (1995),
Abstract;
Synthesis of charybdotoxin and of two N-terminal truncated analogues. Structural and functional characterisation: C. Vita, et al.; Eur. J. Biochem.
217, 157 (1993),
Abstract;
Characterization of high affinity binding sites for charybdotoxin in human T lymphocytes. Evidence for association with the voltage-gated K+ channel: C. Deutsch, et al.; J. Biol. Chem.
266, 3668 (1991),
Abstract;
Design, synthesis, and functional expression of a gene for charybdotoxin, a peptide blocker of K+ channels: C.S. Park, et al.; PNAS
88, 2046 (1991),
Abstract;
Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins: F. Bontems, et al.; Science
254, 1521 (1991),
Abstract;
Characterization of high affinity binding sites for charybdotoxin in synaptic plasma membranes from rat brain. Evidence for a direct association with an inactivating, voltage-dependent, potassium channel: J. Vazquez, et al.; J. Biol. Chem.
265, 15564 (1990),
Abstract;
Full Text
Potassium channel toxins: P.N. Strong; Pharmacol. Ther.
46, 137 (1990), (Review),
Abstract;
Solution synthesis of charybdotoxin (ChTX), a K+ channel blocker: P. Lambert, et al.; BBRC
170, 684 (1990),
Abstract;
Characterization of high affinity binding sites for charybdotoxin in sarcolemmal membranes from bovine aortic smooth muscle. Evidence for a direct association with the high conductance calcium-activated potassium channel: J. Vazquez, et al.; J. Biol. Chem.
264, 20902 (1989),
Abstract;
Full Text
Charybdotoxin inhibits proliferation and interleukin 2 production in human peripheral blood lymphocytes: M. Price et al.; PNAS
86, 10171 (1989),
Abstract;
Mutant potassium channels with altered binding of charybdotoxin, a pore-blocking peptide inhibitor: R. MacKinnon & C. Miller; Science
245, 1382 (1989),
Abstract;
Toxins in the characterization of potassium channels: N.A. Castle, et al.; TINS
12, 59 (1989),
Abstract;
Purification, sequence, and model structure of charybdotoxin, a potent selective inhibitor of calcium-activated potassium channels: G. Gimenez-Gallego, et al.; PNAS
85, 3329 (1988),
Abstract;
Purification of charybdotoxin, a specific inhibitor of the high-conductance Ca2+-activated K+ channel: C. Smith, et al.; J. Biol. Chem.
261, 14607 (1986),
Abstract;
Full Text
Charybdotoxin, a protein inhibitor of single Ca2+-activated K+ channels from mammalian skeletal muscle: C. Miller, et al.; Nature
313, 316 (1985),
Abstract;
