Inhibitor of protein phosphatase 1 (PP1) (IC50=1.8nM), protein phosphatase 2A (PP2A) (IC50=0.026nM) and to a lesser extent protein phosphatase 2B (PP2B) (IC50=8.7µm). Similar to microcystin-LR (Prod. No. ALX-350-012) but with increased water solubility. Genotoxic. Hepatoxic. Induces oxidative DNA damage by oxidation of purines. Induces apoptosis in HepG2 cells.
Product Specification
| Formula: | C41H60N8O10 |
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| MW: | 825.0 |
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| Source: | Isolated from Nodularia spumigena. |
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| CAS: | 118399-22-7 |
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| RTECS: | GU2294250 |
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| Purity: | ≥95% (HPLC) |
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| Identity: | Identity determined by MS. |
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| Appearance: | Dry residue containing traces of monobasic potassium phosphate. |
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| Solubility: | Soluble in methanol:water (1:1). |
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| Shipping: | Ambient |
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| Long Term Storage: | -20°C |
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Product Literature References
Uptake and accumulation of Microcystin-LR based on exposure through drinking water: An animal model assessing the human health risk: B. Greer, et al.; Sci. Rep.
8, 4913 (2018),
Abstract;
Full Text
Simple, high efficiency detection of microcystins and nodularin-R in water by fluorescence polarization immunoassay: H. Zhang, et al.; Anal. Chim. Acta
992, 119 (2017),
Abstract;
Comparative effects of nodularin and microcystin-LR in zebrafish: 1. Uptake by organic anion transporting polypeptide Oatp1d1 (Slco1d1): S. Faltermann, et al.; Aquat. Toxicol.
171, 69 (2016),
Application(s): Cellular uptake and immunoblotting,
Abstract;
Comparative effects of nodularin and microcystin-LR in zebrafish: 2. Uptake and molecular effects in eleuthero-embryos and adult liver with focus on endoplasmic reticulum stress: S. Faltermann, et al.; Aquat. Toxicol.
171, 77 (2016),
Application(s): Induced ER-stress and TNFα in liver organ cultures of zebrafish,
Abstract;
Nodularin induces tumor necrosis factor-alpha and mitogen-activated protein kinases (MAPK) and leads to induction of endoplasmic reticulum stress: N. Meili, et al.; Toxicol. Appl. Pharmacol.
300, 25 (2016),
Application(s): Cell culture,
Abstract;
Rapid and Sensitive Analysis of Microcystins using Ionic Liquid-based in situ Dispersive Liquid-Liquid Microextraction: H. Yu, et al.; J. Chromatogr. A
1406, 10 (2015),
Application(s): Cell Culture,
Abstract;
On the chemistry, toxicology and genetics of the cyanobacterial toxins, microcystin, nodularin, saxitoxin and cylindrospermopsin: L. Pearson, et al.; Mar. Drugs
8, 1650 (2010),
Abstract;
Full Text
Nodularin-induced genotoxicity following oxidative DNA damage and aneuploidy in HepG2 cells: A. Lankoff, et al.; Toxicol. Lett.
164, 239 (2006),
Abstract;
Bacterial degradation of microcystins and nodularin: S. Imanishi, et al.; Chem. Res. Toxicol.
18, 591 (2005),
Abstract;
Genotoxic potential of Microcystin-LR and nodularin in vitro in primary cultured rat hepatocytes and in vivo in rat liver: N. Bouaicha, et al.; Environ. Toxicol.
20, 341 (2005),
Abstract;
Study on the distribution of nodularin in tissues and cell level in mice: Z. Zhang, et al.; Zhonghua Yu Fang Yi Xue Za Zhi
36, 100 (2002),
Abstract;
The microcystins and nodularins: cyclic polypeptide inhibitors of PP1 and PP2A: B.M. Gulledgea, et al.; Curr. Med. Chem.
9, 1991 (2002),
Abstract;
Detection of nodularin in flounders and cod from the Baltic Sea: V. Sipia, et al.; Environ. Toxicol.
16, 121 (2001),
Abstract;
Influence of microcystin-YR and nodularin on the activity of some proteolytic enzymes in mouse liver: A. Lankoff & A. Kolataj; Toxicon
39, 419 (2001),
Abstract;
Nodularin-Har: a new nodularin from Nodularia: K. Saito, et al; J. Nat. Prod.
64, 139 (2001),
Abstract;
Isolation and detection of microcystins and nodularins, cyanobacterial peptide hepatotoxins: J. Meriluoto, et al.; Methods Mol. Biol.
145, 65 (2000),
Abstract;
Degradation of the cyanobacterial hepatotoxin, nodularin, under light and dark conditions: H. Twist & G.A. Codd; FEMS Microbiol. Lett.
151, 83 (1997),
Abstract;
Cyanobacterial nodularin is a potent inhibitor of type 1 and type 2A protein phosphatases: R.E. Honkanen, et al.; Mol. Pharmacol.
40, 577 (1991),
Abstract;
In vitro and in vivo effects of protein phosphatase inhibitors, microcystins and nodularin, on mouse skin and fibroblasts: R. Matsushima, et al.; BBRC
171, 867 (1990),
Abstract;
Inhibition of protein phosphatases by microcystins and nodularin associated with hepatotoxicity: S. Yoshizawa, et al.; J. Cancer Res. Clin. Oncol.
116, 609 (1990),
Abstract;
Internal surface reversed-phase high-performance liquid chromatographic separation of the cyanobacterial peptide toxins microcystin-LA, -LR, -YR, -RR and nodularin: J.A. Meriluoto, et al.; J. Chromatogr.
509, 390 (1990),
Abstract;
Rapid purification of the peptide toxins microcystin-LR and nodularin: C. Martin, et al.; FEMS Microbiol. Lett.
56, 1 (1990),
Abstract;
Nodularin, microcystin and the configuration of Adda: K.L. Rinehart, et al.; JACS 110, 8557 (1988),
Toxicity and partial structure of a hepatotoxic peptide produced by the cyanobacterium Nodularia spumigena Mertens emend. L575 from New Zealand: W.W. Carmichael, et al.; Appl. Environ. Microbiol.
54, 2257 (1988),
Abstract;
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