- Alomone Labs α-Conotoxin GI inhibits the muscle (α1/β1/δ/γ) nAChR channels heterologously expressed in Xenopus oocytes.A. Time course of α-Conotoxin GI (#STC-500) action on α1/β1/δ/γ 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 1 mM acetylcholine every 100 seconds. 100 nM α-Conotoxin GI were perfused during the period marked by the bar. B. Superimposed traces of α1/β1/δ/γ nAChR channel current in the absence and presence of 100 nM α-Conotoxin GI (taken from the experiment in A).
α-Conotoxin GI is a 13 amino acid peptidyl toxin isolated from the Conus geographus (Geography cone) venom1,2,3. It belongs to the Conotoxin A superfamily and reversibly blocks α/δ nicotinic ACh channel receptors (nAChR).
α-Conotoxin GI reversibly inhibits the high affinity α/δ site on mouse muscle-derived BC3H-1 receptor, a nAChR expressed on postsynaptic membranes4,5. Other low site (α/γ site) on nicotinic receptors from Torpedo californica electric organ is also inhibited by α-Conotoxin GI5.
α-Conotoxin GI (#STC-500) is a highly pure, synthetic, and biologically active peptide toxin.