inhibitor tablets for phosphatase, phosphatase inhibitor tablets




pkg of 10 tablets (04906845001)
pkg of 20 tablets (04906837001)




aqueous buffer: soluble

shipped in

wet ice

storage temp.


General description

PhosSTOP tablets are a proprietary blend of phosphatase inhibitors, formulated as a ready-to-use tablet which dissolves quickly in aqueous solutions (buffers), including buffers containing formalin (for formalin fixation).


Protects proteins against dephosphorylation. Inhibits phosphatase classes such as acid and alkaline phosphatases, as well as serine/threonine (PP1, PP2A, and PP2B) and tyrosine protein phosphatases (PTP) in bacterial, mammalian, yeast, and plant extracts.


PhosSTOP protects protein extracts against dephosphorylation. The tablets inhibit a broad spectrum of phosphatases such as acidic and alkaline phosphatases, as well as serine/threonine (PP1, PP2A, and PP2B), dual-specificity phosphatases and tyrosine protein phosphatases (PTP) in bacterial, insect, mammalian, yeast, and plant extracts. PhosSTOP Tablets are well suited for the purification and detection of phoshorylated proteins. They are also used to prevent dephosphorylation in formalin-fixed paraffin embedded (FFPE) tissue sections.
PhosSTOP tablets can be applied in combination with cOmplete Protease Inhibitor Cocktail Tablets to simultaneously protect proteins against dephosphorylation and proteolytic degradation. Both inhibitor tablets maintain their activity when used together.
PhosSTOP inhibitors were evaluated for their effect on protein assays. The inhibition shows almost no influence on BCA or Bradford protein assays.
PhosSTOP has been used as a component of
  • lysis buffer for the lysis of frozen mouse tissue to obtain protein supernatant
  • lysis of bone derived macrophages
  • nuclear extraction buffer for cell lysis and immunoprecipitation

Features and Benefits

Achieve immediate, effective, and convenient inhibition of a broad spectrum of phosphatases across a wide range of sample materials (e.g., mammalian, plant, yeast, and bacteria) with non-toxic PhosSTOP Phosphatase Inhibitor Cocktail Tablets. PhosSTOP is a proprietary blend of phosphatase inhibitors, formulated as a ready-to-use, quick-dissolving, water-soluble tablet.

  • Comprehensive protection: Inhibit acid and alkaline phosphatases, as well as serine/threonine (PP1, PP2A, and PP2B) and tyrosine protein phosphatases.
  • Safe: Dissolve the non-toxic PhosSTOP Tablets in aqueous solutions and avoid organic solvents (e.g., DMSO).
  • Suitable for formalin fixation: Maintain phosphorylation status of proteins in histological sections.
  • Convenient: Eliminate the time-consuming search for just the right phosphatase inhibitor.
  • Easy to use: Simply drop a quick-dissolving tablet into your buffer.
  • Stable: Store stock solutions for 1 month at +2 to +8°C, or for at least 6 months at -15 to -25°C.

For all-inclusive protein protection, combine PhosSTOP with cOmplete or cOmplete ULTRA Protease Inhibitor Tablets to inhibit both phosphatases and proteases.

Preparation Note

Working concentration: 1 tablet per 10 ml cell extract or buffer
Working solution: Solvent is recommended in distilled water or aqueous buffers (including buffers containing formalin).
Dissolve one tablet per 10 ml aqueous buffer. Alternatively, prepare a 10x stock solution in 1 ml dist. water or 100 mM phosphate buffer, pH 7.0. Higher concentrations of stock solutions (e.g., 20x) are possible.
Storage conditions (working solution): 2 to 8 °C

Other Notes

For life science research only. Not for use in diagnostic procedures.

Legal Information

PhosSTOP is a trademark of Roche


NONH for all modes of transport

The SMX DNA repair tri-nuclease
Wyatt HDM, et al.
Molecular Cell, 65(5), 848-860 (2017)
Piliang Hao et al.
PloS one, 6(2), e16884-e16884 (2011-03-05)
Protein post-translational modifications (PTMs) are regulated separately from protein expression levels. Thus, simultaneous characterization of the proteome and its PTMs is pivotal to an understanding of protein regulation, function and activity. However, concurrent analysis of the proteome and its PTMs...
Expression of siglec-E alters the proteome of lipopolysaccharide (LPS)-activated macrophages but does not affect LPS-driven cytokine production or toll-like receptor 4 endocytosis
Nagala M, et al.
Frontiers in Immunology, 8, 1926-1926 (2018)
Huperzine A ameliorates obesity-related cognitive performance impairments involving neuronal insulin signaling pathway in mice
Wang HY, et al.
Acta Pharmacologica Sinica, 1-1 (2019)
Fabio P S Santos et al.
Blood, 115(6), 1131-1136 (2009-12-17)
Few treatment options exist for patients with myelofibrosis (MF), and their survival is significantly shortened. Activating mutation of the JAK2 tyrosine kinase (JAK2(V617F)) is found in approximately 50% of MF patients. CEP-701 is a tyrosine kinase inhibitor that inhibits JAK2...
Get maximum protection after protein isolation by using protease and phosphatase inhibitor cocktail tablets from Roche.
Read More
Related Content
The phosphatase inhibitors included in PhosSTOP Tablets can be deactivated or removed from a lysate using dialysis.
Read More
An overview of cell lysis and protein extraction methods including detergent solubilization, freeze-thaw lysis, osmotic shock, sonication, enzymatic cell lysis, and mechanical disruption techniques such as Dounce, Polytron, and mortar and pestle homogenization.
Read More

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon


Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.