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Merck

495609

Okadaic Acid, Prorocentrum sp.

InSolution, ≥95%, inhibitor of protein phosphatase 1

別名:

InSolution Okadaic Acid, Prorocentrum sp.

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この商品について

実験式(ヒル表記法):
C44H68O13
分子量:
805.00
UNSPSC Code:
12352106
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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

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.

Biochem/physiol Actions

Cell permeable: no
Primary Target
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

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).

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.
Gjertsen, B.T., et al. 1994. J. Cell Sci.107, 3363.
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.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Toxicity: Toxic (F)

保管分類

10 - Combustible liquids

wgk

WGK 1

flash_point_f

188.6 °F - closed cup - (Dimethylsulfoxide)

flash_point_c

87 °C - closed cup - (Dimethylsulfoxide)


適用法令

試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。

Group 4: Flammable liquids + Type 3 petroleums + Hazardous rank III + Water insoluble liquid

fsl

495609-25UG:

jan


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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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