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About This Item
Empirical Formula (Hill Notation):
C324H478N94O90S8
Molecular Weight:
7386.36
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.32
Recommended Products
form
solid
Quality Level
shipped in
dry ice
storage temp.
−20°C
Gene Information
human ... CACNA1G(8913) , CACNA1H(8912) , CACNA1I(8911)
mouse ... CACNA1G(12291) , CACNA1H(58226) , CACNA1I(239556)
rat ... CACNA1G(29717) , CACNA1H(114862) , CACNA1I(56827)
Amino Acid Sequence
Lys-Ile-Asp-Gly-Tyr-Pro-Val-Asp-Tyr-Trp-Asn-Cys-Lys-Arg-Ile-Cys-Trp-Tyr-Asn-Asn-Lys-Tyr-Cys-Asn-Asp-Leu-Cys-Lys-Gly-Leu-Lys-Ala-Asp-Ser-Gly-Tyr-Cys-Trp-Gly-Trp-Thr-Leu-Ser-Cys-Tyr-Cys-Gln-Gly-Leu-Pro-Asp-Asn-Ala-Arg-Ile-Lys-Arg-Ser-Gly-Arg-Cys-Arg-Ala
General description
Kurtoxin is hydrophobic in nature and shares sequence identity with α-scorpion and has cysteine-stabilized α-helix and β-sheet (CSαβ) motif. It interacts with N-type, and P-type calcium (Ca2+) channels as well.
Application
Kurtoxin has been used as a blocker of T-type and R-Type voltage-gated calcium channels (VGGCs) in hippocampal neurons.
Biochem/physiol Actions
Kurtoxin is isolated from the venom of the South African scorpion Parabuthus transvaalicus. It associates with voltage-gated sodium channels and delays their inactivation.
T-type Ca2+ channel blocker; Scorpion toxin
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Chul Won Lee et al.
Biochemistry, 51(9), 1862-1873 (2012-02-15)
Kurtoxin is a 63-amino acid polypeptide isolated from the venom of the South African scorpion Parabuthus transvaalicus. It is the first and only peptide ligand known to interact with Cav3 (T-type) voltage-gated Ca(2+) channels with high affinity and to modify
Giulietta Pinato et al.
Journal of cellular physiology, 220(3), 727-747 (2009-05-15)
Blockage of GABA-A receptors in hippocampal neuronal cultures triggers synchronous bursts of spikes initiating neuronal plasticity, partly mediated by changes of gene expression. By using specific pharmacological blockers, we have investigated which sources of Ca2+ entry primarily control changes of
Serguei S Sidach et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 22(6), 2023-2034 (2002-03-16)
Studies of Ca channels expressed in oocytes have identified kurtoxin as a promising tool for functional and structural studies of low-threshold T-type Ca channels. This peptide, isolated from the venomous scorpion Parabuthus transvaalicus, inhibits low-threshold alpha1G and alpha1H Ca channels
R S Chuang et al.
Nature neuroscience, 1(8), 668-674 (1999-04-10)
The biophysical properties of T-type voltage-gated calcium channels are well suited to pacemaking and to supporting calcium flux near the resting membrane potential in both excitable and non-excitable cells. We have identified a new scorpion toxin (kurtoxin) that binds to
Chul Won Lee et al.
Biochemical and biophysical research communications, 416(3-4), 277-282 (2011-11-19)
Kurtoxin, a 63-amino acid peptide stabilized by four disulfide bonds, is the first reported peptide inhibitor of T-type voltage-gated calcium channels. Although T-type calcium channels have been implicated in a number of disease states, including epilepsy, chronic pain, hypertension and
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