|Related Categories||Bioactive Small Molecules, Cell Biology, Cell Signaling and Neuroscience, Kinase/Phosphatase Biology, O,|
|solubility||DMSO: ≥1 mg/mL|
|ethanol: ≥1 mg/mL|
|methanol: ≥1 mg/mL|
|shipped in||dry ice|
Isolated from unialgal cultures of dinoflagellates.
Dinoflagellate toxin and an ionophore-like polyether derivative of a 38 carbon, fatty acid. Readily enters cells. Inhibitor of type 1 and type 2A protein phosphatases. Does not inhibit tyrosine phosphatases, alkaline phosphatases or acid phosphatase. Known tumor promotor. Used to study various cellular processes including cell cycle, apoptosis, nitric oxide metabolism and calcium signaling.
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≥90% (HPLC), solid
≥90% (HPLC), translucent film
≥90% (HPLC), powder
≥90% (HPLC), film
Certificate of Analysis
Certificate of Origin
|Precautionary statements||P261-P280-P301 + P310-P311|
|Personal Protective Equipment||Eyeshields, Faceshields, Gloves, type P2 (EN 143) respirator cartridges|
|Hazard Codes (Europe)||T|
|Risk Statements (Europe)||23/24/25-38|
|Safety Statements (Europe)||26-36/37-45|
|RIDADR||UN 3462 6.1 / PGI|
Phosphoprotein phosphatases, which hydrolyze the phosphoester bonds of phosphoserines, phosphothreonines or phosphotyrosines, play an essential role in signal transduction and actively contribute to ...
Keywords: Catalysis, Cloning, Gene expression, Neurotransmitters, Phosphorylations, Transduction
Protein Kinase C-Mediated Phosphorylation Of A Single Serine Residue On The Rat Glial Glutamine Transporter SN1 Governs Its Membrane Trafficking. Nissen-Meyer, L.S., et al. J. Neurosci. 31, 6565-75, (2011)
Okadaic acid induces Akt hyperphosphorylation and an oxidative stress-mediated cell death in serum starved SK-N-SH human neuroblastoma cells that are augmented by rapamycin. Edelstein J and Rockwell P Neurosci. Lett. 531(2), 74-9, (2012)
Algal toxins and reverse osmosis desalination operations: laboratory bench testing and field monitoring of domoic acid, saxitoxin, brevetoxin and okadaic acid. Seubert EL, Trussell S, Eagleton J, et al. Water Res. 46(19), 6563-73, (2012)
Serine/threonine-protein phosphatase 2A physically interacts with human telomerase reverse transcriptase hTERT and regulates its subcellular distribution. Xi P, Zhou L, Wang M, et al. J. Cell. Biochem. 114(2), 409-17, (2013)
Quantitative determination of the okadaic acid toxins group by a colorimetric phosphatase inhibition assay: interlaboratory study. Smienk H, Domínguez E, Rodríguez-Velasco ML, et al. J. AOAC Int. 96(1), 77-85, (2013)
Comparative toxicological study of the novel protein phosphatase inhibitor 19-Epi-okadaic acid in primary cultures of rat cerebellar cells. Fernández-Sánchez MT, Cabrera-García D, Ferrero-Gutierrez A, et al. Toxicol. Sci. 132(2), 409-18, (2013)
D-Glucose modulates intestinal Niemann-Pick C1-like 1 (NPC1L1) gene expression via transcriptional regulation. Malhotra P, Boddy CS, Soni V, et al. Am. J. Physiol. Gastrointest. Liver Physiol. 304(2), G203-10, (2013)
Kidins220 accumulates with tau in human Alzheimer's disease and related models: modulation of its calpain-processing by GSK3β/PP1 imbalance. López-Menéndez C, Gamir-Morralla A, Jurado-Arjona J, et al. Hum. Mol. Genet. 22(3), 466-82, (2013)
Effects of okadaic acid on haemocytes from Mytilus galloprovincialis: a comparison between field and laboratory studies. Prado-Alvarez M, Flórez-Barrós F, Sexto-Iglesias A, et al. Mar. Environ. Res. 81, 90-3, (2012)
Protein phosphatase 2A is expressed in response to colony-stimulating factor 1 in macrophages and is required for cell cycle progression independently of extracellular signal-regulated protein kinase activity. Wilson N.J., et al. Biochem. J. 339, 517-524, (1999)
Inhibitors of protein phosphatase 1 and 2A differentially regulate the expression of inducible nitric-oxide synthase in rat astrocytes and macrophages. Pahan, K., et al. J. Biol. Chem. 273, 12219-12226, (1998)
Dephosphorylation and deactivation of Ca2+/calmodulin-dependent protein kinase II in betaTC3-cells is mediated by Mg2+- and okadaic-acid-sensitive protein phosphatases. Easom, R.A., et al. Biochem. J. 329, 283-288, (1998)
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