Every lot is tried & tested in a relevant biological assay.
- Middleton, R.E. et al. (2002) Biochemistry 41, 14734.
- Hall, E.O. et al. (2010) FASEB J. 24, 608.14.
- Alomone Labs ProTx-II-Biotin inhibits NaV1.7 channels expressed in Xenopus oocytes.A. Time course of ProTx-II-Biotin (#STP-100-B) inhibition of NaV1.7 channels 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 inhibited by 200 nM ProTx-II-Biotin (bar), applied for 4.5 min. B. Superimposed traces of NaV1.7 current upon application of control and of 200 nM ProTx-II-Biotin (as indicated), taken from the recording shown in A.
- Alomone Labs ProTx-II-Biotin specifically binds avidin.SDS-PAGE resolved purified ProTx-II-Biotin (#STP-100-B) specifically binds peroxidase-conjugated avidin, showing a dose-dependent ECL signal at ~4 kDa, absent for the same amount of unlabeled ProTx-II (#STP-100).
ProTx-II is a peptidyl toxin originally produced in Thrixopelma pruriens, the Peruvian green velvet tarantula. It was identified as a voltage-gated Na+ channel (NaV) blocker which inhibits both tetrodotoxin-sensitive and tetrodotoxin-resistant channels1.
Binding of ProTx-II to an extracellular domain of NaV channel, probably to a hydrophobic site3, inhibits current by shifting the channel activation to more positive potentials1-2.
ProTx-II Inhibits NaV1.2, NaV1.3, NaV1.5, NaV1.6, NaV1.7, and NaV1.8. It is a significantly more potent inhibitor against NaV1.7 than the other NaV channel subtypes1.
ProTx-II was also found as an effective modulator which shifts the voltage dependence activity of T-type Ca2+channel1.