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Tautomycin

Inhibitor of PP1 and PP2A
 
ALX-380-041-C025 25 µg 214.00 USD
 
ALX-380-041-C050 50 µg 307.00 USD
 
ALX-380-041-C100 100 µg 589.00 USD
Do you need bulk/larger quantities?
 
Replaces Prod. #: BML-EI243

Cell permeable protein phosphatase inhibitor. Inhibits PP1 completely at 3nM and PP2 at 30nM. Inhibition of PP2B is over 10.000 fold weaker and PP2C is not inhibited. Structurally similar to okadaic acid but has opposite relative potency for PP1 and PP2A. Its cell permeability and unique inhibitory profile make tautomycin a useful tool for identifying phosphatase subtypes and physiological substrates for PP2 and PP2A. Treatment of MCF7 cells (breast caner line) with 10µM produced time-dependent inhibition of PP1 (~80% in 6h, 100% in 14 h), with only 20% inhibition of PP2A after 24h.

Product Specification

Formula:C41H66O13
 
MW:767.0
 
Source:Isolated from Streptomyces spiroverticillatus.
 
CAS:109946-35-2
 
RTECS:WX1000000
 
Purity:≥85% (HPLC)
 
Appearance:Colorless film.
 
Solubility:Soluble in 100% ethanol, methanol or DMSO.
 
Shipping:Ambient
 
Long Term Storage:-20°C
 
Handling:Protect from light and moisture.
 
ALX-380-041
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ALX-380-041

Product Literature References

Protein Phosphatase 1 Beta is Modulated by Chronic Hypoxia and Involved in the Angiogenic Endothelial Cell Migration: D. Iacobazzi, et al.; Cell. Physiol. Biochem. 36, 384 (2015), Application(s): Cell Culture, Migration Assay, Abstract; Full Text
IRBIT governs epithelial secretion in mice by antagonizing the WNK/SPAK kinase pathway: D. Yang, et al.; J. Clin. Invest. 121, 956 (2011), Abstract; Full Text
The epsilon hinge-ear region regulates membrane localization of the AP-4 complex: L. Paolini, et al.; Traffic 12, 1604 (2011), Abstract;
Apparent PKA activity responds to intermittent hypoxia in bone cells: a redox pathway?: Y.L. Zhang, et al.; Am. J. Physiol. Heart Circ. Physiol. 299, H225 (2010), Abstract; Full Text
Phosphorylation of huntingtin at Ser421 in YAC128 neurons is associated with protection of YAC128 neurons from NMDA-mediated excitotoxicity and is modulated by PP1 and PP2A: M. Metzler, et al.; J. Neurosci. 30, 14318 (2010), Abstract; Full Text
Effects of H2O2 at rat myenteric neurones in culture: E. Pouokam, et al.; Eur. J. Phamacol. 615, 40 (2009), Abstract;
The apoptosis-inducing activity of the two protein phosphatase inhibitors, tautomycin and thyrsiferyl 23-acetate, is not due to the inhibition of protein phosphatases PP1 and PP2A: K. Kikuchi, et al.; Int. J. Mol. Med. 4, 395 (1999), Review, Abstract;
Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin-A, okadaic acid, and tautomycin: B. Favre et al.; J. Biol. Chem. 272, 13856 (1997), Abstract;
Molecular shape analysis and activity of tautomycin, a protein phosphatase inhibitor: Y. Sugiyama, et al.; Bioorg. Med. Chem. Lett. 6, 3 (1996),
Effects of tautomycin, a protein phosphatase inhibitor, on recycling of mammalian cell surface molecules: T. Kurisaki et al.; J. Antibiot. (Tokyo) 45, 252 (1992), Abstract;
Myosin light chain phosphatase activities and the effects of phosphatase inhibitors in tonic and phasic smooth muscle: M.C. Gong, et al.; J. Biol. Chem. 267, 14662 (1992), Abstract; Full Text
Structurally different members of the okadaic acid class selectively inhibit protein serine/threonine but not tyrosine phosphatase activity: M. Suganuma, et al.; Toxicon 30, 873 (1992), Abstract;
A novel protein phosphatase inhibitor, tautomycin. Effect on smooth muscle: M. Hori et al.; FEBS Lett. 285, 145 (1991), Abstract;
M. Ubukata et al.; J. Chem. Soc. Chem. Commun. 244 (1990),
Tautomycin from the bacterium Streptomyces verticillatus. Another potent and specific inhibitor of protein phosphatases 1 and 2A: C. MacKintosh & S. Klumpp; FEBS Lett. 277, 137 (1990), Abstract;
Comparison of the effect of tautomycin and phorbol ester on protein kinase C in a cell-free system: J. Magae, et al.; J. Antibiot. 42, 1290 (1989), Abstract;
A new antibiotic, tautomycin: X.C. Cheng, et al.; J. Antibiot. (Tokyo) 40, 907 (1987), Abstract;

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