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方案
>88% (HPLC)
表单
solid
储存温度
−20°C
Amino Acid Sequence
Gly-Val-Ser-Cys-Leu-Cys-Asp-Ser-Asp-Gly-Pro-Ser-Val-Arg-Gly-Asn-Thr-Leu-Ser-Gly-Thr-Leu-Trp-Leu-Tyr-Pro-Ser-Gly-Cys-Pro-Ser-Gly-Trp-His-Asn-Cys-Lys-Ala-His-Gly-Pro-Thr-Ile-Gly-Trp-Cys-Cys-Lys-Gln [Disulfide bridges: 4-46, 6-36, 29-47]
一般描述
Synthetic peptide toxin that was originally isolated from the sea anemone, Anthopleura xanthogrammica.
Synthetic peptide toxin.
应用
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.
生化/生理作用
Anthopleurin-A slows the repolarization phase of nerve and muscle action potentials by inactivating the sodium channel.[1] Anthopleurin-A shows a preference towards cardiac channels over the neuronal sodium channels.[2] It is a toxin used to study the gating mechanisms of sodium channels.[1]
Shown to have inotropic effects and not chronotropic effects on mammalian heart preparations.
其他说明
supplied as trifluoroacetate salt
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
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
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
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
Mark Restivo et al.
Journal of cardiovascular electrophysiology, 15(3), 323-331 (2004-03-20)
The occurrence of significant spatial dispersion of repolarization in vivo as it relates to the mechanism of arrhythmia formation in the long QT syndrome (LQTS) continues to be questioned. We investigated a guinea pig model of LQT3 using anthopleurin-A (AP-A)
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