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Leiurotoxin I,Catalog Number: K1100-V,Store at -20°C or -80°C,Lyophilized
Leiurotoxin-1 (Scyllatoxin) is a neurotoxin that was originally isolated from Leiurus quinquestriatus hebraeus. Leiurotoxin-1 binds and blocks SK channels (small conductance Ca2+-activated K+ channels) in the brain and spinal cord and inhibits them.
Leiurotoxin I is a 31-residue peptide (sequence AFCNLRMCQLSCRSLGLLGKCIGDKCECVKH-NH2), with a helix and a short antiparallel β-sheet. This toxin is stabilized by disulfide bonds: Cys8-Cys26 and Cys12-Cys28 is bound to the β-sheet, while Cys3-Cys21 is bound to an N-terminal segment preceding the helix. Leiurotoxin adopts the ά/β motif. Especially the positively charged residues (Arg6 and Arg13, which are located in the ά helix) are important for the expression of toxin biological activities and for its receptor affinity.
Scyllatoxin is a blocker of small-conductance Ca2+– activated K+ channels at 10−13–10−11 M concentrations in various cell types. This toxin shows similarity in its physiological activity and binding specificity to apamin, but both toxins show no structural similarity.
Scyllatoxin blocks the slow after-hyperpolarization that follows an action potential in some nerve cells.
Scyllatoxin induces spontaneous contractions in guinea pig taenia coli muscle cells that have been relaxed with epinephrine.
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Leiurotoxin I,Catalog Number: K1100-V,Store at -20°C or -80°C,Lyophilized
Leiurotoxin-1 (Scyllatoxin) is a neurotoxin that was originally isolated from Leiurus quinquestriatus hebraeus. Leiurotoxin-1 binds and blocks SK channels (small conductance Ca2+-activated K+ channels) in the brain and spinal cord and inhibits them.
Leiurotoxin I is a 31-residue peptide (sequence AFCNLRMCQLSCRSLGLLGKCIGDKCECVKH-NH2), with a helix and a short antiparallel β-sheet. This toxin is stabilized by disulfide bonds: Cys8-Cys26 and Cys12-Cys28 is bound to the β-sheet, while Cys3-Cys21 is bound to an N-terminal segment preceding the helix. Leiurotoxin adopts the ά/β motif. Especially the positively charged residues (Arg6 and Arg13, which are located in the ά helix) are important for the expression of toxin biological activities and for its receptor affinity.
Scyllatoxin is a blocker of small-conductance Ca2+– activated K+ channels at 10−13–10−11 M concentrations in various cell types. This toxin shows similarity in its physiological activity and binding specificity to apamin, but both toxins show no structural similarity.
Scyllatoxin blocks the slow after-hyperpolarization that follows an action potential in some nerve cells.
Scyllatoxin induces spontaneous contractions in guinea pig taenia coli muscle cells that have been relaxed with epinephrine.