Overview
Leu33 - C-terminal amidation
- Sousa, S.R. et al. (2019) PlosONE 12(9), e0182848.
Centrifuge all products before use (10000 x g 5 min).
Alomone Labs Cd1a Toxin inhibits NaV1.7 channel currents heterologously expressed in Xenopus oocytes.A. Representative time course of Cd1a Toxin (#STC-260) 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 significantly inhibited by application of 200 nM Cd1a Toxin (green).
B. Superimposed traces of NaV1.7 channel current in the absence (black) and presence (green) of 200 nM Cd1a Toxin (taken from the recording in A).
Cd1a Toxin (β-theraphotoxin-Cd1a) is a spider toxin, isolated from the venom of the African rear-horned baboon tarantula Ceratogyrus darlingi, a spider species that is mostly native to southern Africa1.
Cd1a Toxin was shown to be a potent blocker of Nav1.7 channel and has a modest activity on CaV2.2 channels. Cd1a Toxin reversed spontaneous pain behaviours induced in mice by activation of NaV1.7, demonstrating its analgesic potential1. Physiological and pharmacological studies have demonstrated that Cav channels, including CaV2.2 and a number of NaV channels, including NaV1.7, are involved in nociceptive signaling, playing a critical role in the development of chronic pain associated with tissue and nerve injury1.
Cd1a Toxin belongs to NaSpTx family 1, a class of promiscuous toxins that can modulate a range of ion channels, including NaV, CaV, KV, mechanosensitive and proton-gated ion channels. The primary structure of Cd1a strongly suggests that it will fold into an ICK motif that is expected to provide a high level of chemical, thermal and biological stability1.
