Protease and phosphatase inhibitor cocktails and tablets are ideal for the protection of proteins during extraction or lysate preparation from primary cells, cultured mammalian cells, animal tissues, plant tissues, yeast or bacterial cells. Individual protease inhibitors are also available separately and in multiple sizes. Formulations with or without EDTA are available for divalent cation-sensitive assays.

  • Effective—outperforms leading competitor formulations across targeted protease and phosphatase families
  • Multiple package sizes—liquid cocktails and tablets are available in multiple sizes and formats to accommodate different volume and pricing needs
  • Improved formulation—tablets dissolve more quickly into a clear solution, and are fully compatible with all Pierce protein assays.
  • Convenient—refrigerator-stable formulations are easier to use than individual inhibitors
  • Complete protection—all-in-one formulations contain both protease and phosphatase inhibitors (combined cocktail only)
  • Compatible—does not interfere with protein assays or other downstream applications

Choose a broad spectrum cocktail or individual inhibitor

Inhibitor component Target (mechanism) Liquid cocktails and tablet inhibitors
Protease Phosphatase Combined
AEBSF∙HCL Serine protease (irreversible)

Aprotinin Serine protease (irreversible)


Bestatin Aminopeptidase (reversible)


E-64 Cysteine (irreversible)


Leupeptin Serine and cysteine protease (reversible)


Pepstatin Aspartic acid proteases (reversible)

PMSF Serine proteases (irreversible)      
EDTA†* Metalloproteases


Sodium fluoride* Serine-threonine and acidic phosphatases  

Sodium orthovanadate* Tyrosine and alkaline phosphatases  

Β-glycero-phosphate* Serine-threonine phosphatases  

Sodium pyrophosphate* Serine-threonine phosphatases  

†Not in EDTA-free formulations
*Not available individually

Compare protease inhibitor cocktails and tablets

Figure 1. Comparison of commercially available protease inhibitor cocktails and tablets. Pancreatic extract (50 μL, 1 μg/μL protein) or trypsin (25 μL, 0.1 units/μL) was incubated with a quenched-fluorescent, protease-cleavable substrate for cysteine (A) or serine proteases (B) in the presence or absence of commercially available protease inhibitors with EDTA-containing (blue) or EDTA-free (purple) formulations. Reactions were incubated for two hours at 37°C and the fluorescence determined at indicated detecting emissions. The percent protease inhibition is shown for each protease inhibitor formulation.

Figure 2. Protein phosphorylation is preserved in cell and tissue extracts. Relative levels of total and phosphorylated protein from extracts prepared in the absence or presence of phosphatase inhibitors were determined by western blot analysis. (A): AKT and PDGFR in serum-starved, PDGF-stimulated (100 ng/mL) NIH 3T3 cell extracts. (B): ERK1/2 in liver and spleen tissue extracts. (C): the degree of inhibition for protein, acid and alkaline phosphatase activity was determined in mouse brain extract after treatment with Pierce Phosphatase Inhibitor Tablets or another commercially available phosphatase inhibitor tablet. Percent inhibition is indicated.