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About This Item
Empirische Formel (Hill-System):
C324H478N94O90S8
Molekulargewicht:
7386.36
MDL-Nummer:
UNSPSC-Code:
12352202
NACRES:
NA.32
Empfohlene Produkte
Form
solid
Qualitätsniveau
Versandbedingung
dry ice
Lagertemp.
−20°C
Angaben zum Gen
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
Allgemeine Beschreibung
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.
Anwendung
Kurtoxin has been used as a blocker of T-type and R-Type voltage-gated calcium channels (VGGCs) in hippocampal neurons.
Biochem./physiol. Wirkung
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
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
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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
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
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
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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