Other · Peptide neurotoxin
Charybdotoxin
Also known as CTX
Charybdotoxin is a 37-amino-acid peptide from scorpion venom used as a selective blocker of several types of potassium channels in research.
- Length
- 37 amino acids
- Half-life
- Not well characterised
- Mechanism
- It potently blocks large-conductance Ca2+-activated (BK), voltage-gated (Kv1.3), and intermediate-conductance (IKCa1) potassium channels.
- Studied in
- Employed in electrophysiology studies to isolate and characterise specific potassium channel currents in various cell preparations.
About Charybdotoxin
Charybdotoxin is a peptide neurotoxin isolated from the venom of the scorpion Leiurus quinquestriatus hebraeus. Its structure consists of 37 amino acids cross-linked by three disulfide bridges, forming a stable conformation that allows it to bind with high affinity to the outer vestibule of specific potassium channels.
As a potent and relatively selective channel blocker, Charybdotoxin serves as a valuable pharmacological tool. Its application in research allows for the functional dissection of cellular processes involving its target channels, such as T-lymphocyte activation through Kv1.3 and neuronal excitability regulated by BK channels.
Laboratory notes
- Highly potent; handle with appropriate laboratory precautions for toxic compounds.
- Reconstitute in high-purity water or appropriate buffer; aqueous solutions can be stored frozen.
- The three disulfide bridges are critical for the peptide's tertiary structure and biological activity.
Storage and reconstitution basics: storage guide.
Questions about Charybdotoxin
What is the primary use of Charybdotoxin in a lab setting?
It is used as a highly selective pharmacological tool to block specific potassium channels, enabling the study of their function in cellular physiology and excitability.
Which potassium channels does Charybdotoxin primarily block?
It is known to block large-conductance calcium-activated (BK) channels and certain voltage-gated potassium channels, such as Kv1.3, with high affinity.
What is the structural significance of its disulfide bonds?
The three disulfide bonds are essential for maintaining the correct three-dimensional fold of the peptide, which is required for its high-affinity binding to the channel pore.
Is Charybdotoxin for human use?
No. It is supplied strictly for in-vitro laboratory research and is not for human or animal consumption.
Related research peptides
All products are sold for laboratory research use only. Not for human consumption, not a medicine, not for diagnosing, treating or preventing any condition.