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Ca2+-activated K+ channel blocker
ALX-630-059-C100 100 µg 487.00 USD
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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
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)
MI:14: 2046
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.
Shipping:Ambient Temperature
Long Term Storage:-20°C
Regulatory Status:RUO - Research Use Only

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;

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