459620
Okadaic Acid sodium salt
≥98% (TLC), solid,film (colorless), protein phosphatase 2A and protein phosphatase 1 inhibitor, Calbiochem®
别名:
冈田酸,钠盐
产品名称
冈田酸,钠盐, Water-soluble analog of Okadaic Acid. Inhibits protein phosphatases 1 and 2A.
质量水平
方案
≥98% (TLC)
表单
solid
制造商/商品名称
Calbiochem®
储存条件
OK to freeze
protect from light
颜色
white to off-white
溶解性
water: 1 mg/mL
DMSO: 20 mg/mL
ethanol: 20 mg/mL
运输
ambient
储存温度
−20°C
一般描述
冈田酸的水溶性类似物(目录号495604)。抑制蛋白磷酸酶1和2A。
生化/生理作用
产物不与ATP竞争。
可逆:否
细胞渗透性:否
靶标IC50:蛋白磷酸酶1、蛋白磷酸酶2A分别为10-15 nM、0.1 nM
其他说明
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.
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法律信息
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
免责声明
毒性:有毒(F)
警示用语:
Danger
危险分类
Acute Tox. 3 Dermal - Acute Tox. 3 Inhalation - Acute Tox. 3 Oral - Skin Irrit. 2
储存分类代码
6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
WGK
WGK 3
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
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
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
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
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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