Overview
- Lee, S. et al. (2010) Mol. Pain 6, 97.
Alomone Labs ω-Conotoxin FVIA inhibits CaV2.2 channel expressed in Xenopus oocytes.A. Time course of ω-Conotoxin FVIA (#STC-780) action on CaV2.2 (α1B + α2δ1 + β1 subunits) maximum peak current amplitude. 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 ramp to +50 mV elicited in 2 mM Ba2+. 50 nM ω-Conotoxin FVIA was perfused as indicated by the bar (green) for 5 min. B. Superimposed examples of CaV2.2 channel maximum peak current in the absence (control) and presence (green) of 50 nM ω-Conotoxin FVIA (taken from the experiment in A).
- Lee, S. et al. (2010) Mol. Pain 6, 97.
- Adams, D.J. et al. (2013) Biochim. Biophys. Acta. 1828, 1619.
ω-Conotoxins are disulfide-rich peptides comprised of 24–31 amino acids, isolated from the venom of marine predatory cone snails. They have a high content of basic amino acid residue and common cysteine scaffold that stabilizes the four-loop framework1,2.
ω-Conotoxin FVIA is originally isolated from Conus Fulmen. It is a selective, potent and reversible voltage-gated N-Type Ca2+ (CaV2.2) channel blocker that preferentially blocks nociception in inflammatory pain models, and allodynia and hyperalgesia in neuropathic pain models1,2. Studies have shown that ω-Conotoxin FVIA demonstrates analgesic potency and greater reversibility for the treatment of refractory pain and low side effects1.
Voltage-gated N-Type Ca2+ channels are predominantly expressed in nerve terminals and are involved in the regulation of neuronal excitability and nociceptive signals. They are able to transduce electrical activity into other cellular functions and regulate calcium homeostasis2.
ω-Conotoxin FVIA (#STC-780) is a highly pure, synthetic, and biologically active peptide toxin.
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