Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing (PubMed:31402191). This toxin acts on human Nav1.4/SCN4A and Nav1.6/SCN8A voltage-gated sodium channels (PubMed:31402191). Expressed by the venom gland. Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta). Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family.