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459620

Sigma-Aldrich

Okadaic Acid sodium salt

≥98% (TLC), solid,film (colorless), protein phosphatase 2A and protein phosphatase 1 inhibitor, Calbiochem®

Synonyme(s) :

Okadaic Acid, Sodium Salt

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About This Item

Formule empirique (notation de Hill):
C44H67O13 · Na
Poids moléculaire :
826.98
Code UNSPSC :
12352106
Nomenclature NACRES :
NA.77

product name

Okadaic Acid, Sodium Salt, Water-soluble analog of Okadaic Acid. Inhibits protein phosphatases 1 and 2A.

Niveau de qualité

Pureté

≥98% (TLC)

Forme

solid

Fabricant/nom de marque

Calbiochem®

Conditions de stockage

OK to freeze
protect from light

Couleur

white to off-white

Solubilité

water: 1 mg/mL
DMSO: 20 mg/mL
ethanol: 20 mg/mL

Conditions d'expédition

ambient

Température de stockage

−20°C

Description générale

Water-soluble analog of Okadaic Acid (Cat. No. 495604). Inhibits protein phosphatases 1 and 2A.

Actions biochimiques/physiologiques

Cell permeable: no
Product does not compete with ATP.
Reversible: no
Target IC50: 10-15 nM, 0.1 nM against protein phosphatase 1, protein phosphatase 2A, respectively

Avertissement

Toxicity: Toxic (F)

Autres remarques

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.
Normura, 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.W. 1989. J. Biol. Chem.254 21435.
Haystead, T.A. et al. 1989. Nature337, 78.

Informations légales

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

Pictogrammes

Skull and crossbones

Mention d'avertissement

Danger

Mentions de danger

Classification des risques

Acute Tox. 3 Dermal - Acute Tox. 3 Inhalation - Acute Tox. 3 Oral - Skin Irrit. 2

Code de la classe de stockage

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

Classe de danger pour l'eau (WGK)

WGK 3


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

K Kiguchi et al.
Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research, 5(9), 995-1004 (1994-09-01)
To investigate a possible relationship between apoptosis induction and protein phosphorylation in human breast carcinoma cells, we treated three such cell types, MB-231, MCF-7, and AU-565, with okadaic acid (OA), an inhibitor of protein phosphatases 1 and 2A, or phorbol
Q Song et al.
Journal of cellular physiology, 153(3), 550-556 (1992-12-01)
Gamma-radiation, tetrandrine, bistratene A, and cisplatin were all found to induce pronounced morphological changes characteristic of apoptosis and extensive DNA fragmentation in the human BM13674 cell line 8 h after treatment. Apoptosis induced in BM13674 cells by these diverse agents
Protein phosphatases come of age.
P Cohen et al.
The Journal of biological chemistry, 264(36), 21435-21438 (1989-12-25)
Y Tada et al.
Immunopharmacology, 24(1), 17-24 (1992-07-01)
Okadaic acid is a potent tumor promoter and an inhibitor of serine/threonine-specific protein phosphatases. We studied the effect of okadaic acid in human T cell activation and phosphorylation of internal substrates. Okadaic acid at up to 4 nM enhanced phorbol
M Nomura et al.
Biochemistry, 31(47), 11915-11920 (1992-12-01)
Smooth muscle myosin light chain kinase is phosphorylated at two sites (A and B) by different protein kinases. Phosphorylation at site A increases the concentration of Ca2+/calmodulin required for kinase activation. Diphosphorylated myosin light chain kinase was used to determine

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