Calyculin A
Chemical Name: N-[(3S)-[4-(1E)-3-[(2R,3R,4R,7S,8S,9R)-2-[(1S,3S,4S,5R,7E,9E,11E,13Z)-14-Cyano-3,5-dihydroxy-1-methoxy-4,6,8,9,13-pentamethyl-7,9,11,13-tetradecatetraenyl]-9-hydroxy-4,4,8-trimethyl-3-(phosphonooxy)-1,6-dioxaspiro[4.5]dec-7-yl]-1-propenyl]-2-oxazoly]butyl]-4-deoxy-4-(dimethylamino)-5-O-methyl-L-ribonamide
Purity: ≥97%
Biological Activity
Calyculin A is a potent and selective cell-permeable inhibitor of protein phosphatase 1 (IC50 = 0.3 - 0.7 nM) and protein phosphatase 2A (IC50 = 0.5 - 1 nM). Displays > 10,000,000-fold selectivity over PP2B and PP2C.Note: This product is typically prepared in DMSO.
Technical Data
The technical data provided above is for guidance only.
For batch specific data refer to the Certificate of Analysis.
Tocris products are intended for laboratory research use only, unless stated otherwise.
Background References
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Calyculin A and okadaic acid: inhibitors of protein phosphatase activity.
Ishihara et al.
Biochem.Biophys.Res.Commun., 1989;159:871 -
Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin-A, okadaic acid, and tautomycin.
Favre et al.
J.Biol.Chem., 1997;272:13856 -
Serine-threonine protein phosphatase inhibitors: development of therapeutic strategies.
McCluskey et al.
J.Med.Chem., 2002;45:1151 -
The binding mode of calyculin A to protein phosphatase-1.
Lindval et al.
J.Biol.Chem., 1997;272:23312
Product Datasheets
Citations for Calyculin A
The citations listed below are publications that use Tocris products. Selected citations for Calyculin A include:
9 Citations: Showing 1 - 9
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NMDAR-Activated PP1 Dephosphorylates GluN2B to Modulate NMDAR Synaptic Content.
Authors: Chiu Et al.
Cell Rep 2019;28:332
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Transient PP2A inhibition alleviates normal tissue stem cell susceptibility to cell death during radiotherapy.
Authors: Fabbrizi Et al.
Cell Death Dis 2018;9:492
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In vivo brain GPCR signaling elucidated by phosphoproteomics.
Authors: Liu
Science 2018;360(6395):eaao4927
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Phosphatases control PKA-dependent functional microdomains at the outer mitochondrial membrane.
Authors: Burdyga Et al.
Proc Natl Acad Sci U S A. 2018;115(28):E6497
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Selective inhibition of the kinase DYRK1A by targeting its folding process.
Authors: Kii Et al.
Nat Commun 2016;7:11391
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Mechanical coupling between transsynaptic N-cadherin adhesions and actin flow stabilizes dendritic spines.
Authors: Chazeau Et al.
J Neurochem 2015;26:859
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PYK2 selectively mediates signals for growth versus differentiation in response to stretch of spontaneously active vascular smooth muscle.
Authors: Bhattachariya Et al.
Physiol Rep 2014;2
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Pain modulators regulate the dynamics of PKA-RII phosphorylation in subgroups of sensory neurons.
Authors: Isensee Et al.
J Cell Sci 2014;127:216
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Nitric oxide relaxes circular smooth muscle of rat distal colon through RhoA/Rho-kinase independent Ca2+ desensitisation.
Authors: Colpaert Et al.
Br J Pharmacol 2005;144:588
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