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- Berecki, G. et al. (2010) Mol. Pharmacol. 77, 139.
- Alomone Labs ω-Conotoxin CVIF inhibits CaV2.2 channel currents expressed in Xenopus oocytes.A. Time course of ω-Conotoxin CVIF (#STC-770) action on maximum CaV2.2 channel (α1B + α2δ1 + β1) current elicited in 2 mM Ba2+. 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 +40 mV. 50 nM ω-Conotoxin CVIF were perfused as indicated by the bar (green) for 2.5 min. B. Superimposed examples of CaV2.2 channel maximum peak current in the absence (control) and presence (green) of 50 nM ω-Conotoxin CVIF (taken from the experiment in A).
- Berecki, G. et al. (2010) Mol. Pharmacol. 77, 139.
- Sadeghi, M. et al. (2013) Mol. Pain 9, 51.
ω-Conotoxin CVIF is a peptide toxin originally isolated from Conus catus venom. It selectively blocks voltage-gated N-type Ca2+ channel and is being tested as a potential drug for the treatment of chronic and neuropathic pain. CVIF has a higher affinity for Ca2+ channels in their inactivated state.
Neuronal (N)-type voltage-gated Ca2+channels (VGCCs) are involved in regulating neuronal excitability and nociceptive signals and play an important role in the transduction of acute and chronic pain perception. The VGCC channel residues that directly interact with ω-conotoxins, act at or near the outer vestibule of N-type (CaV2.2) and P/Q-type (CaV2.1) VGCCs1.
CVIF can prevent the conduction of nociceptive signals from the peripheral to the central nervous system by inhibiting neurotransmitter release from primary afferent nerve terminals in the dorsal horn of the spinal cord1,2.
CVIF has the ability to potently and selectively inhibit depolarization-activated Ba2+ currents through recombinant N-type Ca2+ channels in snails’ oocytes1.
ω-Conotoxin CVIF (#STC-770) is a highly pure, synthetic, and biologically active peptide toxin.
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