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Anabaenopeptin A

Inhibitor of protein phosphatase.
ALX-350-183-C100 100 µg 292.00 USD
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Anabaenopeptins are a highly diverse group of bioactive peptides produced by several genera of cyanobacteria such as Anabaena, Planktothrix, Microcystis and Nodularia. These peptides are commonly detected in cyanobacterial blooms along with the well known microcystins. Unique cyclic peptides where lysine is conserved in position 2 and cyclisation is achieved by linkage of the lysine to the C-terminal amino acid. In addition the side chain of a single amino acid is attached via a ureido bond. Bioactive peptides originally isolated from Anabaena flos-aquae NRC 525-17 where they were shown to be non-toxic in mice but had dose dependant relaxations in rat aortic preparations with endothelium precontracted with 0.1µM norpinephrine.
Anabaenopeptins inhibit protein phosphatase.

Product Details

Source:Isolated from Microcystis aeruginosa.
Purity:≥95% (HPLC)
Identity:Identity determined by MS.
Appearance:Pale powder or an oil (film), depending on the lot.
Solubility:Soluble in methanol.
Shipping:Ambient Temperature
Long Term Storage:-20°C
Regulatory Status:RUO - Research Use Only
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Product Literature References

Degradation of Multiple Peptides by Microcystin-Degrader Paucibacter toxinivorans (2C20): A.A. Santos, et al.; Toxins (Basel) 13, 265 (2021), Abstract; Full Text
Cyanobacterial peptides – Nature's own combinatorial biosynthesis: M. Welker &; FEMS Microbiol. Rev. 30, 530 (2006), Abstract;
The presence of microcystins and other cyanobacterial bioactive peptides in aquatic fauna collected from Greek freshwaters: S. Gkelis, et al.; Aquat. Toxicol. 78, 32 (2006), Abstract;
Diversity and distribution of Microcystis (Cyanobacteria) oligopeptide chemotypes from natural communities studied by single-colony mass spectrometry: M. Welker, et al.; Microbiology 150, 1785 (2004), Abstract;
Two cyclic peptides, anabaenopeptins, a third group of bioactive compounds from the cyanobacteriumAnabaena flos-aquae NRC 525-17: K. Harada, et al.; Tetrahed. Lett. 36, 1511 (1994),

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