Overview
- Walewska, A. et al. (2008) J. Am. Chem. Soc. 130, 14280.
Alomone Labs µ-Conotoxin SxIIIA inhibits NaV1.4 currents in Xenopus oocytes.A. Time course of µ-Conotoxin SxIIIA (#STC-645) blocking action on maximum NaV1.4 current amplitude. Maximum peak current amplitudes were plotted as a function of time. Membrane potential was held at -100 mV and oocytes were stimulated by a 100 ms voltage step to 0 mV. 50 nM µ-Conotoxin SxIIIA was perfused as indicated by the bar (green) for 200 sec. B. Superimposed examples of NaV1.4 channel peak current in the absence (control) and presence (green) of 50 nM µ-Conotoxin SxIIIA (taken from the experiment in A).
- McCormack, K. et al. (2013) Proc. Natl. Acad. Sci. U. S. A. 110, E2724.
Voltage-gated sodium (NaV) channels contribute to physiological and pathophysiological electrical signaling in nerve and muscle cells. They play a role in the generation and propagation of action-potential in excitable cells. Eukaryotic NaV channels are heteromeric membrane proteins composed of a pore-forming α-subunit and auxiliary β-subunits1.
µ-Conotoxin SxIIIA is a three-disulfide bridged peptide conotoxin originally isolated from the venom of the Conus striolatus cone snail. SxIIIA is a blocker of the voltage-gated NaV1.4 channel and has an effective concentration of 50-100 nM and an IC50 of 7 nM for the channel. µ-Conotoxin SxIIIA and other toxins derived from venomous animals such as spiders, scorpions, mollusks or plants exhibit promising therapeutic and specifically analgesic properties.
µ-Conotoxin SxIIIA (#STC-645) is a highly pure, synthetic, and biologically active peptide toxin.
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