Batch dependent - please inquire should you have specific requirements.
Buffer
10 mM phosphate buffer, 50 mM NaCl
Preservative
None
Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Introduction
Saxitoxin dihydrochloride is an amorphous hygroscopic solid. Saxitoxin is a neurotoxin that acts as a selective, reversible, voltage-gated sodium channel blocker. One of the most potent known natural toxins, it acts on the voltage-gated sodium channels of neurons, preventing normal cellular function and leading to paralysis.
Keywords
Saxitoxin; STX; neurotoxin; PSP
Citations
Publication ()
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Background
Saxitoxin (STX) is a neurotoxin naturally produced by certain species of marine dinoflagellates (Alexandrium sp., Gymnodinium sp., Pyrodinium sp.) and freshwater cyanobacteria (Dolichospermum cicinale sp., some Aphanizomenon spp., Cylindrospermopsis sp., Lyngbya sp., Planktothrix sp.). Saxitoxin can accumulate in floating invertebrates including molluscs (bivalves and gastropods), crustaceans and echinoderms, and human consumption of contaminated shellfish can lead to paralytic shellfish poisoning (PSP). Saxitoxin was isolated from Saxidomus for the first time, hence its name. It is a powerful neurotoxin and the most famous paralytic shellfish toxin. At present, saxitoxin can also refer to more than 50 structure-related neurotoxins (collectively referred to as "saxitoxins") produced by protozoa, algae, and cyanobacteria. including saxitoxin itself, neosaxitoxin (NSTX), gonyautoxins (GTX) and decarbamoylsaxitoxin (dcSTX).
Saxitoxin is a selective, reversible, voltage-gated sodium channel blocker. As one of the most powerful natural toxins known, it acts on the voltage-gated sodium channels of neurons, organizes normal cell function and leads to paralysis. Voltage-gated sodium channel participates in normal neuronal function. It is distributed on the axon and has four transmembrane domains. When the voltage changes or some ligands combine in the right way, the voltage-gated sodium channel will open. The normal operation of this channel is very important for the transmission of action potentials. When it is affected by saxitoxin, it will not be able to transmit neural signals, resulting in paralysis of the affected area. Saxitoxin reversibly binds to the sodium channel, and the binding site is directly in the pore of the channel protein, blocking the opening and preventing the sodium ions from flowing through the membrane, which leads to the neurological pause described above.
Figure 1. Representation of the molecular structure of saxitoxins, with positive charge fully delocalized over the pyrimidine and imidazole groups (resonance structure representation shown inside the red circles) (Source: Leal JF, et al. 2022)
The LD50 of saxitoxin orally is 5.7μg/kg, the lethal injection dose is about 0.6μg/kg, and the dose of aerosol inhalation is about 5mg·min/m3. saxitoxin can also enter the human body through an open wound with a lethal dose of about 50 μg/person.
Alternative Names
STX [OVA]
References
1. Wiese M, et al. Neurotoxic alkaloids: saxitoxin and its analogs. Mar Drugs. 2010 Jul 20;8(7):2185-211.
2. Leal JF, et al. Marine paralytic shellfish toxins: chemical properties, mode of action, newer analogues, and structure-toxicity relationship. Nat Prod Rep. 2022 Jan 26;39(1):33-57.
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References
Marine paralytic shellfish toxins: chemical properties, mode of action, newer analogues, and structure-toxicity relationship
Up to the end of 2020Every year, the appearance of marine biotoxins causes enormous socio-economic damage worldwide. Among the major groups of biotoxins, paralytic shellfish toxins, comprising saxitoxin and its analogues (STXs), are the ones that cause the most severe effects on humans, including death. However, the knowledge that currently exists on their chemistry, properties and mode of toxicological action is disperse and partially outdated. This review intends to systematically compile the dispersed information, updating and complementing it. With this purpose, it addresses several aspects related to the molecular structure of these toxins. Special focus is given to the bioconversion reactions that may occur in the different organisms (dinoflagellates, bivalves, and humans) and the possible mediators involved. A critical review of the most recently discovered analogues, the M-series toxins, is presented. Finally, a deep discussion about the relationship between the molecular structure (e.g., effect of the substituting groups and the net charge of the molecules) and the toxic activity of these molecules is performed, proposing the concept of "toxicological traffic light" based on the toxicity equivalency factors (TEFs)
Paralytic Shellfish Toxins (PST)-Transforming Enzymes: A Review
Toxins (Basel)
Authors: Raposo MIC, Gomes MTSR, Botelho MJ, Rudnitskaya A
Paralytic shellfish toxins (PSTs) are a group of toxins that cause paralytic shellfish poisoning through blockage of voltage-gated sodium channels. PSTs are produced by prokaryotic freshwater cyanobacteria and eukaryotic marine dinoflagellates. Proliferation of toxic algae species can lead to harmful algal blooms, during which seafood accumulate high levels of PSTs, posing a health threat to consumers. The existence of PST-transforming enzymes was first remarked due to the divergence of PST profiles and concentrations between contaminated bivalves and toxigenic organisms. Later, several enzymes involved in PST transformation, synthesis and elimination have been identified. The knowledge of PST-transforming enzymes is necessary for understanding the processes of toxin accumulation and depuration in mollusk bivalves. Furthermore, PST-transforming enzymes facilitate the obtainment of pure analogues of toxins as in natural sources they are present in a mixture. Pure compounds are of interest for the development of drug candidates and as analytical reference materials. PST-transforming enzymes can also be employed for the development of analytical tools for toxin detection. This review summarizes the PST-transforming enzymes identified so far in living organisms from bacteria to humans, with special emphasis on bivalves, cyanobacteria and dinoflagellates, and discusses enzymes' biological functions and potential practical applications.
COA
Publication 
Figure 1. Representation of the molecular structure of saxitoxins, with positive charge fully delocalized over the pyrimidine and imidazole groups (resonance structure representation shown inside the red circles)
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