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Our Bioassay
- Possani, L.D. et al. (1999) Eur. J. Biochem. 264, 287.
Alomone Labs AaH1 Toxin modulates NaV1.2 channels expressed in Xenopus oocytes.A. Representative time course of AaH1 Toxin (#STA-155) effect on the normalized area of NaV1.2 channel current. Membrane potential was held at -100 mV, current was elicited by a 100 ms voltage step to 0 mV every 10 sec and was significantly enhanced by the application of 1 µM AaH1 Toxin (green). B. Superimposed traces of NaV1.2 current after application of control (black) and of 1 µM AaH1 Toxin (green), taken from the recording in A.
- Possani, L.D. et al. (1999) Eur. J. Biochem. 264, 287.
- Fabrichny, I.P. et al. (2012) J. Biol. Chem. 287, 14136.
- di Tommaso, A. et al. (2012) J. Biol. Chem. 287, 1414.
- Chow, C.Y. et al. (2015) Toxins 7, 2494.
AaH1 Toxin is a low molecular weight peptide toxin originally isolated from Androctonus australis scorpion venom. It blocks the fast inactivation phase of voltage-gated Na+ channels1-3. AaH1 Toxin is one of four α-toxins: AahI, AahII, AahIII, and AahIV which account for 95% of the venom lethality2.
There are nine mammalian subtypes of voltage-gated sodium (NaV) channels: NaV1.1–NaV1.9. They are responsible for propagating action potentials in excitable cells and are considered to be important therapeutic targets in numerous pathophysiological conditions such as cardiac arrhythmia and epilepsy4.
AaH1 Toxin (#STA-155) is a highly pure, synthetic, and biologically active peptide toxin.
