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Our Bioassay
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- Wadsworth, J.D. et al. (1994) J. Biol. Chem. 269, 18053.
- Grissmer, S. et al. (1992) J. Gen. Physiol. 99, 63.
- Jager, H. and Grissmer, S. (1997) Cell. Physiol. Biochem. 7, 179.
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Alomone Labs Scyllatoxin inhibits rSK2 channels stably expressed in HEK293T cells.rSK2 channel currents were measured using whole cell voltage clamp in the presence of Ca2+ in the pipette solution. A voltage ramp from -120 mV to +60 mV was applied every 10 sec from a holding potential of -80 mV. A. Time course of current amplitude at 0 mV before (black) and during (green) application of 1 nM Scyllatoxin (#STS-370). B. Representative current traces at control conditions (black) and following 140 s application of 1 nM Scyllatoxin (green), taken from the experiment in A.
Alomone Labs Scyllatoxin inhibits KCa2.2 channels heterologously expressed in Xenopus oocytes.Oocyte membrane potential was held at +5 mV (in a low Cl- solution) and currents were elicited by intraoocyte CaCl2 injection. During the period marked by a green trace (30 seconds), 100 nM of Scyllatoxin (#STS-370) was applied by perfusion.
- 1. Chicchi, G.G. et al. (1988) J. Biol. Chem. 263, 10192.
- 2. Rodriguez de la Vega, R.C. and Possani, L.D. (2004) Toxicon 43, 865.
- 3. Auguste, P. et al. (1992) Biochemistry 31, 648.
- 4. Wadsworth, J.D. et al. (1994) J. Biol. Chem. 269, 18053.
- 5. Grissmer, S. et al. (1992) J. Gen. Physiol. 99, 63.
- 6. Jager, H. and Grissmer, S. (1997) Cell. Physiol. Biochem. 7, 179.
- 7. Auguste, P. et al. (1990) J. Biol. Chem., 265, 4753.
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Scyllatoxin is a 31 amino acid long toxin, originally isolated from the Leiurus quinquestriatus hebraeus scorpion venom, and is classified as α-KTx 5.1 scorpion toxin family, having three disulfide bridges1,2.
Scyllatoxin was shown to compete with 125I-apamin binding in the brain3. Furthermore, Scyllatoxin appears to be selective for apamin-sensitive SK channels. Scyllatoxin inhibits apamin-sensitive SK channel activity in guinea-pig and rabbit hepatocytes4, SK currents in human lymphoblastoma cells5,6, and epinephrine-induced relaxation of visceral smooth muscle7.
Scyllatoxin also inhibits the apamin-sensitive after hyperpolarization that follows action potentials in skeletal muscle7 and neurons8. The SK channel-mediated after hyperpolarising current (IAHP) of dorsal vagal neurons, presuming Kca2.3 (SK3), were blocked by Scyllatoxin (20-30 nM)9. HEK 293 cell currents stably expressing hKca2.1 (hSK1) and Kca2.2 (hSK2) were blocked by Scyllatoxin with an IC50 of 80 nM and 287 pM, respectively10.
Scyllatoxin (#STS-370) is a highly pure, synthetic, and biologically active peptide toxin.