Product Name:IMPERATOXIN-INHIBITOR
Purity:95%
Molar Mass:3.7 kDa
Chemical Formula:C148H260N58O45S6
Storage:Store at -20 degrees Celsius
Sequence:GDCLPHLKRCKADNDCCGKKCKRRGTNAEKRCR
Application:
Imperatoxin-Inhibitor is a synthetic peptide designed to inhibit the activity of imperatoxin, a potent peptide toxin from the venom of the scorpion Pandinus imperator. Imperatoxin primarily targets ryanodine receptors (RyRs), which are critical for calcium release in muscle cells. By blocking imperatoxin’s interaction with RyR1, the Imperatoxin-Inhibitor helps in studying the precise mechanisms of calcium regulation and the role of RyRs in muscle physiology. This inhibitor is essential for research focused on understanding calcium signaling pathways, muscle disorders, and potential therapeutic interventions. With high specificity and stability, Imperatoxin-Inhibitor is an invaluable tool in advanced biochemical and pharmacological studies.
Current Research:
Imperatoxin I (IpTx_i) is a heterodimeric protein isolated from the venom of the African scorpion Pandinus imperator. It comprises two polypeptide subunits: a large subunit of 104 amino acids and a smaller subunit of 27 amino acids, linked by a disulfide bond. The large subunit exhibits phospholipase A₂ (PLA₂) activity, which plays a crucial role in the toxin's function.
IpTx_i specifically targets ryanodine receptors (RyRs), which are intracellular calcium (Ca²⁺) release channels essential for Ca²⁺ signaling in muscle contraction and other cellular processes. Upon binding to RyRs, the PLA₂ activity of IpTx_i hydrolyzes phospholipids in the sarcoplasmic reticulum membrane, releasing fatty acids. These fatty acids interact with RyRs or associated proteins, leading to inhibition of the channel's activity and a consequent decrease in Ca²⁺ release into the cytoplasm. This mechanism effectively modulates intracellular Ca²⁺ levels, impacting muscle contraction and other Ca²⁺-dependent functions.
The unique properties of IpTx_i make it a valuable tool in scientific research, particularly in studies focusing on Ca²⁺ signaling pathways and RyR function. By modulating RyR activity, IpTx_i aids in elucidating the physiological and pathological roles of these channels in muscle physiology and various diseases.
In summary, Imperatoxin I is a scorpion-derived peptide that inhibits ryanodine receptor channels through its PLA₂ activity, leading to reduced Ca²⁺ release from the sarcoplasmic reticulum. Its specific interaction with RyRs provides significant insights into Ca²⁺-mediated cellular processes and offers potential avenues for therapeutic intervention in disorders involving dysregulated Ca²⁺ homeostasis.
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