Overview
Phe34 – C-terminal amidation
- Nicolas, S. et al. (2019) Toxins 11, 367.
Centrifuge all products before use (10000 x g 5 min).
Alomone Labs Phlotoxin 1 inhibits NaV1.7 channel currents heterologously expressed in Xenopus oocytes.A. Representative time course of Phlotoxin 1 (#STP-800) inhibition of NaV1.7 channels current. Membrane potential was held at -80 mV, current was elicited by a 100 ms voltage step to 0 mV every 10 sec, and significantly inhibited by application of 250 nM Phlotoxin 1 (green).
B. Superimposed traces of NaV1.7 channel currents in the absence (control) and presence (green) of 250 nM Phlotoxin 1 (taken from the recording in A).
- Gonçalves, T.C. et al. (2019) Toxins 11, 484.
- Cardoso, F.C. and Lewis, R.J. (2019) Front. Pharmacol. 10, 366.
- Nicolas, S. et al. (2019) Toxins 11, 367.
- Klint, J.K. et al. (2015) Br. J. Pharmacol. 172, 2445.
Phlotoxin 1 (PhlTx1) is a voltage-gated Na+ channel (NaV) blocker, originally isolated from the venom of a Phlogiellus genus spider endemic to Papua New Guinea.
Phlotoxin 1, characterized by a 34-amino acids sequence with 3 disulfide bridges and structure around the inhibitory cysteine-knot (ICK) architectural motif, was shown to belong to the spider toxin NaSpTx family 11,2.
Nav1.7 was identified as the most sensitive ion channel and main target for Phlotoxin 1 inhibition3. NaV1.7 channel plays an important role in human pain signaling pathway and it is an important therapeutic target for treatment of chronic pain. Hence, Phlotoxin 1 is an important candidate for the study of pain, pain treatment, and development of analgesics. It is also an interesting toxin in order to decipher the involvement of Nav1.7 in cellular excitability and pain3,4.
Phlotoxin 1 ((#STP-800) is a highly pure, synthetic and biologically active peptide toxin.
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