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  • 產品名稱：rlberiotoxin(IbTx)

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簡單介紹：
rlberiotoxin(IbTx)
詳情介紹：
Sequence QFTDVDCSVS KECWSVCKDL FGVDRGKCMG KKCRCYQ.
Specificity Iberiotoxin is a potent selective blocker of the high conductance Ca2+-activated K+ channels (maxi-K).
Characteristics Source: Mesobuthus tamulus (Eastern Indian scorpion).
Molecular formula: C179H277N51O55S7.
Disulfide bonds between Cys7-Cys28, Cys13-Cys33, and Cys17-Cys35.
Purity > 98 %
Background Inhibition of BKCa channels heterologously expressed in HEK293 cells by Iberiotoxin. mSlo channel currents, before and during application of 100nM rIberiotoxin. The mSlo currents were activated by a 50 ms voltage step to +100 mV from a prepulse of -180 mV with intracellular 10 M Ca2+.
Molecular Weight 4248
Application Notes 50-100 nM
Comment

K+ channel toxin -KTx 1.3
Restrictions For Research Use only
Format Lyophilized
Reconstitution Any aqueous buffer. Centrifuge all product preparations before use (10000 x g 5 min).
Concentration after reconstitution: Dissolving 50 g in 1.175ml will provide a stock solution of 10 M.
Handling Advice Soluble in Water.
Supplier Images
image for rlberiotoxin (IbTx) (ABIN1001697) mSlo channel currents, before and during application of 100nM rIberiotoxin. The mSlo ...
Background publications Meera, Wallner, Toro: "A neuronal beta subunit (KCNMB4) makes the large conductance, voltage- and Ca2+-activated K+ channel resistant to charybdotoxin and iberiotoxin." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 97, Issue 10, pp. 5562-7, 2000 (PubMed).

Product cited in: Koschak, Koch, Liu, Kaczorowski, Reinhart, Garcia, Knaus: "[125I]Iberiotoxin-D19Y/Y36F, the first selective, high specific activity radioligand for high-conductance calcium-activated potassium channels." in: Biochemistry, Vol. 36, Issue 7, pp. 1943-52, 1997 (PubMed).

Galvez, Gimenez-Gallego, Reuben, Roy-Contancin, Feigenbaum, Kaczorowski, Garcia: "Purification and characterization of a unique, potent, peptidyl probe for the high conductance calcium-activated potassium channel from venom of the scorpion Buthus tamulus." in: The Journal of biological chemistry, Vol. 265, Issue 19, pp. 11083-90, 1990 (PubMed).