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Nodularin

Inhibitor of PP1 and PP2A
 
ALX-350-061-C050 50 µg 60.00 USD
 
ALX-350-061-C100 100 µg 87.00 USD
 
ALX-350-061-C250 250 µg 190.00 USD
 
ALX-350-061-M001 1 mg 649.00 USD
Do you need bulk/larger quantities?
 
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
 
MW:825.0
 
Source:Isolated from Nodularia spumigena.
 
CAS:118399-22-7
 
RTECS:GU2294250
 
Purity:≥95% (HPLC)
 
Identity:Identity determined by MS.
 
Appearance:Dry residue containing traces of monobasic potassium phosphate.
 
Solubility:Soluble in methanol:water (1:1).
 
Shipping:Ambient
 
Long Term Storage:-20°C
 
350-061
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350-061

Product Literature References

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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