Overview
- Abbas, N. et al. (2008) Biochem. Biophys. Res. Commun. 376, 525.
Alomone Labs Aam-KTX inhibits KV1.3 channel currents expressed in Xenopus oocytes.A. Time course of Aam-KTX (#STA-110) action on KV1.3 channels current. Peak current amplitude recorded at +55 mV was plotted as a function of time. Membrane potential was held at -100 mV and oocytes were stimulated by a 100 ms voltage ramp to +60 mV. 0.5 nM Aam-KTX was perfused as indicated by the bar (green). B. Superimposed examples of KV1.3 channel current in the absence (control) and presence (green) of 0.50 nM Aam-KTX (taken from the experiment in A).
KTxs are scorpion peptide toxins that act on voltage-gated K+ channels which can be divided into four groups: α, β, γ, and κ. Aam-KTX is an analogue of Kaliotoxin that originates from Androctonus amoreuxi scorpion venom. It contains a conserved α-helix/β-sheet structural motif composed of a single α-helix and one β-sheet of two antiparallel strands. KTxs primarily affects voltage-gated Shaker-related and ether-a-go-go-related gene (ERG) K+ channels and Ca2+-activated K+ channels of high, intermediate, or small conductance1,2. IC50 values of Aam-KTX for KV1.3 channel and KV1.2 are 1.1 ± 0.02 and 10.4 ± 1.5 nM, respectively1.
Potassium channels are a large family of membrane proteins ubiquitously distributed in excitable and nonexcitable cells. These channels play a major role in different physiological processes1.
Aam-KTX (#STA-110) is a highly pure, synthetic, and biologically active peptide toxin.
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