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- Luo, S. et al. (2010) The J. Biol. Chem. 285, 12355.
- Alomone Labs α-Conotoxin LtIA inhibits α3/β2 nAChR channels heterologously expressed in Xenopus oocytes.A. Time course of α-Conotoxin LtIA (#STC-550) action on α3/β2 nAChR channels. Current amplitudes were plotted as a function of time. Membrane potential was held at –60 mV and oocytes were stimulated by exposure to 100 μM acetylcholine and 1 μM atropine, for 1 second every 50 seconds. 2 µM α-Conotoxin LtIA was perfused during the period marked by the bar. B. Superimposed traces of α3/β2 nAChR channel current in the absence and presence of 2 μM α-Conotoxin LtIA (taken from the experiment in A).
- Luo, S. et al. (2010) The J. Biol. Chem. 285, 12355.
α-Conotoxin LtIA is a 16 amino acid peptidyl toxin isolated from the Conus litteratus (Lettered cone) venom1. It belongs to the α-Conotoxin superfamily, although it lacks the highly conserved Ser-Xaa-Pro sequence. It reversibly blocks α3/β2 nicotinic ACh channel receptor with an IC50 of 9.8 nM1.
Little or no block was obtained by 10 fold concentrations of the toxin on α4/β2 and α3/ß4 nicotinic ACh receptors1.
α-Conotoxin LtIA was substantially less potent on α6/α3/β4 versus α6/α3/β2/β3 nAChRs. In contrast, there was little or no block by α-Conotoxin LtIA at 10 µM on other nAChR, including α1/β1/δ/ε, α2/β2, α2/β4, α4/β2, α4/β4, α7, and α9/α101.
α-Conotoxin LtIA (#STC-550) is a highly pure, synthetic, and biologically active peptide toxin.
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