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rScyllatoxin

貨號 Cat. No.
RTS-370
規格 Size
5 μg 5x5 μg 10μg 10μgx10μg 0.1mg

Description

rScyllatoxin



Novel Blocker of KCa2 (SK) K+ Channels












Product#: RTS-370

























Sizes:
5 mg
5 x 5 mg
10 mg
5 x 10 mg
0.1 mg
 














M.W.: 3424










Sequence:

AFCNLRMCQL SCRSLGLLGK CIGDKCECVK H









NMR structure of Scyllatoxin (1SCY).11 Scyllatoxin belongs to the a-KTX-5.2 scorpion toxin family. 2










Purity: >98%












Bioassay:
Inhibition of KCa2.2 channels expressed in Xenopus oocytes by rScyllatoxin and by rMaurotoxin.











Inhibition of KCa2.2 channels expressed in Xenopus oocytes by rScyllatoxin and by rMaurotoxin.

Continuous current recording at holding potential +5 mV with low Cl- content in the bath solution. An outward current (upward deflection) carried out by K+ ions flowing via KCa2.2 channels develops following an intra-oocyte Ca2+ injection (arrow). Both recombinant toxins partially and reversibly depressed the K+ current at 200 nM. Periods of toxin perfusion are marked by the horizontal bars.







 









References:


















































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.

8.


 Goh, J.W. et al. (1992) Brain Res. 591. 165.

9.


 Pedarzani, P. et al. (2000) J. Physiol. 527, 283.

10.


 Strobaek, D. et al. (2000) Br. J. Pharmacol. 129, 991.

11.

Martins, J.C. et al. (1995) J. Mol. Biol. 253, 590.


Scyllatoxin is a 31 amino acid long toxin, originally isolated from the venom of the scorpion Leiurus quinquestriatus hebraeus, and is classified as a-KTx 5.1 scorpion toxin family, having three disulfide bridges.1,2

Scyllatoxin was shown to compete with 125I -apamin binding in the brain.3 Furthermore, Scyllatoxin appears to be selective for apamin-sensitive SK channels. Scyllatoxin inhibits apamin-sensitive SK channel activity in guinea-pig and rabbit hepatocytes,4 SK currents in human lymphoblastoma cells,5,6 and epinephrine-induced relaxation of visceral smooth muscle.7 Scyllatoxin also inhibits the apamin-sensitive afterhyperpolarization that follow action potentials in skeletal muscle7 and neurons.8 The SK channel-mediated Afterhyperpolarising current (IAHP) of dorsal vagal neurons, presuming Kca2.3 (SK3), were blocked by Scyllatoxin (20?0nM).9 HEK 293 cell currents stably expressing hKca2.1 (hSK1) and Kca2.2 (hSK2) were blocked by scyllatoxin with IC50 of 80 nM and 287 pM, respectively.10


 


Scyllatoxin seems to be a very potent blocker of either KCa channels with highest affinity towards Kca2.2, having the following affinities: Kca2.2 < < Kca2.3 < Kca2.1.


 


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