产品名称
Okadaic Acid, Prorocentrum sp., InSolution, ≥95%, inhibitor of protein phosphatase 1
assay
≥95% (HPLC)
form
liquid
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
desiccated (hygroscopic)
protect from light
shipped in
wet ice
storage temp.
−20°C
Quality Level
Biochem/physiol Actions
Cell permeable: no
Primary Target
protein phosphatase
protein phosphatase
Product does not compete with ATP.
Reversible: no
Target IC50: 10-15 nM against protein phosphatase 1; 0.1 nM against protein phosphatase 2A
Disclaimer
Toxicity: Toxic (F)
General description
An ionophore-like polyether derivative of a C38 fatty acid compound isolated from dinoflagellates that have fed on the marine sponge Halinchrondria okadai. It is a potent non-comepetitive, reversible inhibitor of serine/threonine-specific protein phosphatases 1 (PP1, IC50 = 10-15 nM, rabbit skeletal muscle, catalytic subunit) and 2A (PP2A, IC50 = 0.1 nM, rabbit skeletal muscle, catalytic subunit). It has only a trivial effect on protein phosphatase 2B (IC50 = 5 µM), a Ca2+/calmodulin-dependent enzyme, while PP2C, a Mg2+ dependent enzyme, is unaffected. Okadaic acid has no significant effect on the activities of tyrosine phosphatases, alkaline phosphatase, acid phosphatase, and inositol trisphosphatase. It is also a non-phorbol ester-type tumor promoter on mouse skin. Useful for the study of protein phosphatases and of PP1/PP2A in cell extracts, as well as in intact cells. Induces apoptosis in human breast carcinoma (MB-231 and MCF-7) and in myeloid cells, but inhibits glucocorticoid-induced apoptosis in T-cell hybridomas. Has marked contractile effect on smooth muscles and heart muscles. Implicated as a causative agent of diarrhetic shellfish poisoning.
Other Notes
Due to the nature of the Hazardous Materials in this shipment, additional shipping charges may be applied to your order. Certain sizes may be exempt from the additional hazardous materials shipping charges. Please contact your local sales office for more information regarding these charges.
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Haystead, T.A., et al. 1989. Nature337, 78.
Kiguchi, K., et al. 1994. Cell Growth Differentiation5, 995.
Ohaka, Y., et al. 1993. Biochem. Biophys. Res. Commun. 197, 916.
Gopalakrishna, R., et al. 1992. Biochem. Biophys. Res. Commun. 189, 950.
Kreienbuhl, P., et al. 1992. Blood80, 2911.
Nomura, M., et al. 1992. Biochemistry31, 11915.
Song, Q., et al. 1992. J. Cell Physiol.153, 550.
Tada, Y., et al. 1992. Immunopharmacol.24, 17.
Cohen, P., et al. 1990. Trends Biochem. Sci.15, 98.
Cohen, P. 1989. Annu. Rev. Biochem.58, 453.
Cohen, P., and Cohen, P.T. 1989. J. Biol. Chem.264, 21435.
Haystead, T.A., et al. 1989. Nature337, 78.
Packaging
Packaged under inert gas
Physical form
A 250 µM (25 µg/124 µl) solution of Okadaic Acid, (Cat. No. 495604) in DMSO.
Preparation Note
Following initial thaw, aliquot and freeze (-20°C).
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
存储类别
10 - Combustible liquids
wgk
WGK 1
flash_point_f
188.6 °F - closed cup - (Dimethylsulfoxide)
flash_point_c
87 °C - closed cup - (Dimethylsulfoxide)
Ilse Delint-Ramirez et al.
Molecular cell, 82(20), 3794-3809 (2022-10-08)
Neuronal activity induces topoisomerase IIβ (Top2B) to generate DNA double-strand breaks (DSBs) within the promoters of neuronal early response genes (ERGs) and facilitate their transcription, and yet, the mechanisms that control Top2B-mediated DSB formation are unknown. Here, we report that
Julia Kamenz et al.
Current biology : CB, 31(4), 794-808 (2020-12-29)
The phosphorylation of mitotic proteins is bistable, which contributes to the decisiveness of the transitions into and out of M phase. The bistability in substrate phosphorylation has been attributed to bistability in the activation of the cyclin-dependent kinase Cdk1. However
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