Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is active on both mammals and insects, since it inhibits inactivation of rNav1.4/SCN4A, hNav1.5/SCN5A, mNav1.6/SCN8A and insect BgNav1 and DmNav1 channels (PubMed:23637230). In vivo, it shows paralytic activity in mice (PubMed:4091860). Expressed by the venom gland. Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta). Does not show activity on rNav1.2/SCN2A (neither peak current reduction, nor inhibition of inactivation) (PubMed:23637230). Adopts a cis conformation at 9-Pro-His-10. Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily.