A7475
Anthopleurin-A trifluoroacetate salt
>88% (HPLC)
Synonim(y):
AP-A trifluoroacetate salt, Anthopleura toxin A trifluoroacetate salt
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Informacje o tej pozycji
Wzór empiryczny (zapis Hilla):
C220H326N64O67S6 · xC2HF3O2
Masa cząsteczkowa:
5131.72 (free base basis)
UNSPSC Code:
12352202
NACRES:
NA.77
MDL number:
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Pozwól nam pomócNazwa produktu
Anthopleurin-A trifluoroacetate salt, >88% (HPLC)
assay
>88% (HPLC)
form
solid
storage temp.
−20°C
Application
Anthopleurin-A is a toxin used to study the gating mechanisms of sodium channels. Anthopleurin-A slows the repolarization phase of nerve and muscle action potentials by inactivating the sodium channel.
Biochem/physiol Actions
Anthopleurin-A slows the repolarization phase of nerve and muscle action potentials by inactivating the sodium channel. Anthopleurin-A shows a preference towards cardiac channels over the neuronal sodium channels. It is a toxin used to study the gating mechanisms of sodium channels.
Shown to have inotropic effects and not chronotropic effects on mammalian heart preparations.
General description
Synthetic peptide toxin that was originally isolated from the sea anemone, Anthopleura xanthogrammica.
Synthetic peptide toxin.
Other Notes
supplied as trifluoroacetate salt
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Klasa składowania
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
S G Priori et al.
Circulation research, 78(6), 1009-1015 (1996-06-01)
The long-QT syndrome (LQTS) is a hereditary disorder characterized by an abnormally prolonged QT interval and by life-threatening arrhythmias. Recently, two of the genes responsible for LQTS have been identified: SCN5A, a voltage-dependent Na+ channel on chromosome 3 (LQT3), and
M F Sheets et al.
The Journal of general physiology, 106(4), 617-640 (1995-10-01)
The gating charge and voltage dependence of the open state to the inactivated state (O-->I) transition was measured for the voltage-dependent mammalian cardiac Na channel. Using the site 3 toxin, Anthopleurin-A (Ap-A), which selectively modifies the O-->I transition (see Hanck
Dorothy A Hanck et al.
Toxicon : official journal of the International Society on Toxinology, 49(2), 181-193 (2006-11-10)
Site-3 toxins are small polypeptide venoms from scorpions, sea anemones, and spiders that bind with a high specificity to the extracellular surface of voltage-gated Na channels. After binding to a site near the S4 segment in domain IV the toxin
G R Benzinger et al.
Pflugers Archiv : European journal of physiology, 434(6), 742-749 (1997-11-05)
Site-3 toxins from scorpion and sea anemone bind to Na channels and selectively inhibit current decay. Anthopleurins A and B (ApA and ApB, respectively), toxins found in the venom of the sea anemone Anthopleura xanthogrammica, bind to closed states of
S A Monks et al.
Structure (London, England : 1993), 3(8), 791-803 (1995-08-15)
The polypeptide anthopleurin-B (AP-B) is one of a number of related toxins produced by sea anemones. AP-B delays inactivation of the voltage-gated sodium channel of excitable tissue. In the mammalian heart, this effect is manifest as an increase in the
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