A6719
ω-Agatoxin IVA
≥90% (HPLC)
Synonym(s):
SNX 290
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About This Item
Empirical Formula (Hill Notation):
C217H360N68O60S10
CAS Number:
Molecular Weight:
5202.25
UNSPSC Code:
12352200
NACRES:
NA.28
MDL number:
Quality Level
assay
≥90% (HPLC)
form
powder
application(s)
metabolomics
vitamins, nutraceuticals, and natural products
storage temp.
−20°C
Gene Information
human ... CACNA1A(773)
mouse ... CACNA1A(12286)
rat ... CACNA1A(25398)
General description
CACNA1A (calcium voltage-gated channel subunit alpha1 A) gene codes for the α1 subunit of neuronal CaV2.1 (P/Q-type) voltage-gated calcium channels. It is expressed throughout the central nervous system (CNS). CACNA1A gene is located on human chromosome 19p13.
Application
ω-Agatoxin IVA has been used in the manipulation of calcium influx. It has also been used in the study to characterize the spontaneous and evoked activity from murine ventral horn cultures on microelectrode arrays.
Biochem/physiol Actions
Toxin found in the venom of the funnel web spider, Agelenopsis aptera. Potent, selective blocker of mammalian P-type voltage-dependent calcium channels.
Mutations in the CACNA1A (calcium voltage-gated channel subunit alpha1 A) gene is responsible for episodic ataxia 2, familial hemiplegic migraine type 1 (FHM1) and spinocerebellar ataxia type 6 (SCA6).
Features and Benefits
This compound was developed by Pfizer. To browse the list of other pharma-developed compounds and Approved Drugs/Drug Candidates, click here.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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New CACNA1A deletions are associated to migraine phenotypes
Grieco GS, et al.
The Journal of Headache and Pain, 19(1), 75-75 (2018)
I M Mintz et al.
Nature, 355(6363), 827-829 (1992-02-27)
Voltage-dependent calcium channels mediate calcium entry into neurons, which is crucial for many processes in the brain including synaptic transmission, dendritic spiking, gene expression and cell death. Many types of calcium channels exist in mammalian brains, but high-affinity blockers are
I M Mintz et al.
Neuron, 9(1), 85-95 (1992-07-01)
The peptide toxin omega-Aga-IVA blocked P-type Ca2+ channel current in rat Purkinje neurons (KD approximately 2 nM) but had no effect on identified T-type, L-type, or N-type currents in a variety of central and peripheral neurons. omega-Aga-IVA blocked a substantial