459620
Okadaic Acid sodium salt
≥98% (TLC), solid,film (colorless), protein phosphatase 2A and protein phosphatase 1 inhibitor, Calbiochem®
Synonym(s):
Okadaic Acid, Sodium Salt
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About This Item
Empirical Formula (Hill Notation):
C44H67O13 · Na
Molecular Weight:
826.98
UNSPSC Code:
12352106
NACRES:
NA.77
Recommended Products
product name
Okadaic Acid, Sodium Salt, Water-soluble analog of Okadaic Acid. Inhibits protein phosphatases 1 and 2A.
Quality Level
Assay
≥98% (TLC)
form
film (colorless)
solid
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
protect from light
color
white
solubility
water: 1 mg/mL
DMSO: 20 mg/mL
ethanol: 20 mg/mL
shipped in
ambient
storage temp.
−20°C
General description
Water-soluble analog of Okadaic Acid (Cat. No. 495604). Inhibits protein phosphatases 1 and 2A.
Biochem/physiol Actions
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
Warning
Toxicity: Toxic (F)
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.
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.
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.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Acute Tox. 3 Dermal - Acute Tox. 3 Inhalation - Acute Tox. 3 Oral - Skin Irrit. 2
Storage Class Code
6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
WGK
WGK 3
Certificates of Analysis (COA)
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P Kreienbühl et al.
Blood, 80(11), 2911-2919 (1992-12-01)
The phosphatase inhibitors okadaic acid and calyculin A were found to elicit or to modify several neutrophil responses, suggesting that dephosphorylation plays a regulatory role. The concentrations of okadaic acid (> or = 1 mumol/L) that were effective on neutrophil
R Gopalakrishna et al.
Biochemical and biophysical research communications, 189(2), 950-957 (1992-12-15)
The cell-permeable inhibitors of type 1 and 2A protein phosphatases, okadaic acid and calyculin-A, induced a redistribution of protein kinase C (PKC) activity and immunoreactivity (40 to 60%) from cytosol to membrane in some cell types. Calyculin-A was 100-fold more
B T Gjertsen et al.
Journal of cell science, 107 ( Pt 12), 3363-3377 (1994-12-01)
The protein phosphatase inhibitors okadaic acid and calyculin A at moderate concentrations induced three types of apoptotic promyelocytic leukemia cell death, distinct with respect to ultrastructure and polynucleotide fragmentation. Calyculin A at higher concentrations (> 50 nM) induced a non-apoptotic
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
Y Ohoka et al.
Biochemical and biophysical research communications, 197(2), 916-921 (1993-12-15)
Glucocorticoids induce apoptosis in murine T cell hybridomas. It was inhibited by okadaic acid and calyculin A, potent inhibitors of protein phosphatase 1 and 2A, but not by 1-norokadaone, a structural analog of okadaic acid without phosphatase inhibitory activity. The
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