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Ca2+-activated K+ channel blocker
ALX-630-058-C100 100 µg 710.00 USD
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Potent and selective blocker of the high conductance Ca2+-activated K+ channels.

Product Details

Alternative Name:IbTx
(Disulfide bonds between Cys7-Cys28, Cys13-Cys33 and Cys17-Cys35)
Source:Synthetic. From Buthus tamulus.
Quantity:0.11mg (25nmol)
Concentration:0.1mM after reconstitution.
Formulation:Lyophilized from aqueous acetic acid solution.
Purity:≥94% (HPLC)
Reconstitution:Do not remove the cap. Inject 260μl distilled water into the vial using a calibrated syringe. Dissolve the contents thouroughly.
Long Term Storage:-20°C
Use/Stability:The undissolved peptide is stable at -20°C for more than 1 year. The aqueous solution should be used within a few weeks.
Handling:After reconstitution, prepare aliquots and store at -20°C.
Regulatory Status:RUO - Research Use Only

Product Literature References

Description and role in proliferation of iberiotoxin-sensitive currents in different human mammary epithelial normal and cancerous cells: S. Roger, et al.; Biochim. Biophys. Acta 1667, 190 (2004), Abstract;
Iberiotoxin-induced block of Ca2+-activated K+ channels induces dihydropyridine sensitivity of ACh release from mammalian motor nerve terminals: M. T. Flink & W. D. Atchison; J. Pharmacol. Exp. Ther. 305, 646 (2003), 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;
Synthesis and biological characterisation of a series of iberiotoxin analogues: J.P. Flinn, et al.; Int. J. Pept. Protein Res. 45, 320 (1995), Abstract;
Synthetic charybdotoxin-iberiotoxin chimeric peptides define toxin binding sites on calcium-activated and voltage-dependent potassium channels: K.M. Gianciacomo, et al.; Biochemistry 32, 2363 (1993), Abstract;
Mode of action of iberiotoxin, a potent blocker of the large conductance Ca(2+)-activated K+ channel: S. Candia, et al.; Biophys. J. 63, 583 (1992), Abstract;
Purification and characterization of a unique, potent, peptidyl probe for the high conductance calcium-activated potassium channel from venom of the scorpion Buthus tamulus: A. Galvez, et al.; J. Biol. Chem. 265, 11083 (1990), Abstract; Full Text

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