VSTX3 was originally isolated from the Grammostola spatulata spider venom and is also isolated from the Phrixotrichus auratus spider venom.
VSTX3 was first isolated and shown to bind through its affinity to the voltage-sensor domain of KvAP channels. VSTX3 also inhibits voltage-gated rat NaV1.3, NaV1.7 and NaV1.8 Na+ channels.
Voltage-gated sodium channels (VGSC, NaV) play a critical role in excitability of nociceptors (pain-sensing neurons). The peripheral-specific sodium channels NaV1.7, NaV1.8 and NaV1.9 are particularly important in the pathophysiology of different pain syndromes and hence, thought to be potential targets for pain therapeutics.
The expression and functional properties of NaV channels in peripheral sensory neurons can be dynamically regulated following axonal injury or peripheral inflammation.
VSTX3 shows high homology to Ceratotoxin-1 (75%), Ceratotoxin-2 (#STC-100) (77%) and Pterinotoxin-1 (#STT-100) (83%).
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