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Charybdotoxin,CAS#:95751-30-7,Catalog Number:K1080-V,Store at -20°C or -80°C
KCa1.1, KV1.2, KV1.3 K+ channels, Charybdotoxin is a potent selective inhibitor of high conductance (maxi-K), different medium and small conductance Ca2+-activated K+ channels, as well as a voltage-dependent K+ channel (KV1.3)1.
The Charybdotoxin family of scorpion toxins is a group of small peptides that has many family members, such as the pandinotoxin, derived from the venom of scorpion Pandinus imperator.
Scorpions such as the deathstalker paralyze their prey by injecting a potent mix of peptide toxins. Charybdotoxin, a 37 amino acid, 4 kDa neurotoxin with the molecular formula C176H277N57O55S7, is one of the peptide toxins that can be extracted from the venom of the scorpion. Its structure is very similar to that of margatoxin. Charybdotoxin contains three disulfide bridges.
Charybdotoxin occludes the pore of calcium-activated voltage-gated shaker K+ channels by binding to one of four independent, overlapping binding sites. It binds both to the open and the closed states. In addition, the block is enhanced as the ionic strength is lowered. This block occurs as the Asn 30 on the CTX interacts with the Asp 381 on the K+ channel. The blockade of K+ channels by the charybdotoxin peptide causes neuronal hyperexcitability. Mutations of the Lys31Gln and the Asn30Gln had the effect of lessening the CTX block of the pore on the shaker channel.
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Charybdotoxin,CAS#:95751-30-7,Catalog Number:K1080-V,Store at -20°C or -80°C
KCa1.1, KV1.2, KV1.3 K+ channels, Charybdotoxin is a potent selective inhibitor of high conductance (maxi-K), different medium and small conductance Ca2+-activated K+ channels, as well as a voltage-dependent K+ channel (KV1.3)1.
The Charybdotoxin family of scorpion toxins is a group of small peptides that has many family members, such as the pandinotoxin, derived from the venom of scorpion Pandinus imperator.
Scorpions such as the deathstalker paralyze their prey by injecting a potent mix of peptide toxins. Charybdotoxin, a 37 amino acid, 4 kDa neurotoxin with the molecular formula C176H277N57O55S7, is one of the peptide toxins that can be extracted from the venom of the scorpion. Its structure is very similar to that of margatoxin. Charybdotoxin contains three disulfide bridges.
Charybdotoxin occludes the pore of calcium-activated voltage-gated shaker K+ channels by binding to one of four independent, overlapping binding sites. It binds both to the open and the closed states. In addition, the block is enhanced as the ionic strength is lowered. This block occurs as the Asn 30 on the CTX interacts with the Asp 381 on the K+ channel. The blockade of K+ channels by the charybdotoxin peptide causes neuronal hyperexcitability. Mutations of the Lys31Gln and the Asn30Gln had the effect of lessening the CTX block of the pore on the shaker channel.