rStromatoxin-1
- 貨號 Cat. No.
- RTS-350
- 規格 Size
- 5 μg 5x5 μg 10μg 10μgx10μg 0.1mg
Description
rStromatoxin-1
A Novel Kv2 Subfamily Inhibitor
| Product#: | RTS-350 |
| Sizes: |
| 5 mg |
| 5 x 5 mg |
| 10 mg |
| 5 x 10 mg |
| 0.1 mg |
Stromatoxin-1 (ScTx-1) is a 34 amino acid peptide that belongs to the structural inhibitor cysteine knot spider peptide family.
Electrophysiological recordings on COS cell expressing voltage-dependent K+ channels show that this toxin
acts as a gating modifier. Native ScTx-1 blocked Kv2.1, Kv2.2, Kv2.1/9.3 and Kv4.2, with IC50 of 12.7nM,
21.4nM, 7.2nM and 1.2nM, respectively. No activity on Kv4.1 and Kv4.3 was observed.1
| M.W.: | 3792 |
| Sequence: | DCTRM FGACR RDSDC CPHLG CKPTS KYCAW DGTI |
| Purity: | >98% by HPLC |
| Bioassay: |
| The biological activity of the rStromatoxin-1 was tested using two-electrode voltage clamp recording from Xenopus oocytes expressing the Kv2.1 channels. |
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rScTx-1 inhibition of KV2.1 channels expressed in Xenopus oocytes. Left: Current responses to 100 ms depolarization to 0 mV from holding potential of ?00 mV, delivered every 10 seconds before (red) and during application of 670 nM rScTx-1. Right: Time course of amplitude inhibition. The horizontal bars indicate the periods of rScTx-1 perfusion. |
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| Model structure of ScTx-1, based on its homology to Hanatoxin1 (1DLH), SGTx (1LA4) and w-Grammotoxin SIA (1KOZ).2 This class of peptides possesses the scaffold of structural inhibitor cysteine knot spider peptide family, which was shown to function as a gating modifier.3 |
| References: |
1. | Escoubas, P. et al. (2002) Mol. Pharmacol. 62, 481. |
2. | Peitsch, M.C. (1996) Biochem. Soc. Trans. 24, 274. |
3. | Shiau, Y.S. (2003), Chem. Res. Toxicol. 16, 1217. |

