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Sigma-Aldrich

Kurtoxin

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100 μG
662,00 €

662,00 €

Voraussichtliches Versanddatum16. April 2025

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100 μG
662,00 €

About This Item

Empirische Formel (Hill-System):
C324H478N94O90S8
Molekulargewicht:
7386.36
MDL-Nummer:
MFCD04119124
UNSPSC-Code:
12352202
NACRES:
NA.32

662,00 €

Voraussichtliches Versanddatum16. April 2025

Form

solid

Qualitätsniveau

200

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)

Verwandte Kategorien

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[1] and shares sequence identity with α-scorpion and has cysteine-stabilized α-helix and β-sheet (CSαβ) motif.[2] It interacts with N-type, and P-type calcium (Ca2+) channels as well.[2]

Anwendung

Kurtoxin has been used as a blocker of T-type and R-Type voltage-gated calcium channels (VGGCs) in hippocampal neurons.[3]

Biochem./physiol. Wirkung

Kurtoxin is isolated from the venom of the South African scorpion Parabuthus transvaalicus.[2] It associates with voltage-gated sodium channels and delays their inactivation.[4]
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)

Hier finden Sie alle aktuellen Versionen:

Analysenzertifikate (COA)

Lot/Batch Number
061M1722V
061M1722
011M1367
099K1572
078K1112

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Die Dokumentenbibliothek aufrufen

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
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
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
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

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