Pierce Protease and Phosphatase Inhibitor Mini Tablets

Thermo Scientific Pierce Protease and Phosphatase Inhibitor Mini Tablets contain both protease inhibitors and phosphatase inhibitors to provide broad-spectrum complete protection from dephosphorylation and proteolytic degradation.

Features of Protease and Phosphatase Inhibitor Mini Tablets:
• Improved formulation—tablets dissolve quickly to form a clear solution
• Economical—more cost effective than other commercially available formulations for equivalent volumes
• Convenient—ready-to-use, fully disclosed, broad-spectrum formulations
• Compatible—use directly with Pierce BCA assays

The Pierce Protease and Phosphatase Inhibitor Mini Tablets contain aprotinin, bestatin, E-64, EDTA, and leupeptin to provide protection from degradation by serine proteases, cysteine proteases, and aspartic acid proteases. To prevent the dephosphorylation activity of serine/threonine and tyrosine phosphatases, each tablet also contains sodium fluoride, sodium orthovanadate, sodium pyrophosphate, and beta-glycerophosphate. Pierce Protease and Phosphatase Inhibitor Tablets are stable at 4°C for up to 12 months, and each tablet is sufficient for 10 mL of solution.

Pierce Protease and Phosphatase Inhibitor Mini Tablets are the first complete inhibitor tablet. Adding one tablet to 10 mL of lysis buffer provides complete protection from protease and phosphatase activity during protein extraction and protein purification. There are two formulations of this inhibitor available, one containing EDTA and one without. While both formulations have metalloprotease inhibitors, an EDTA-free formulation is available for applications that require divalent cations for protein activity. Similarly, EDTA and certain phosphatase inhibitors interfere with immobilized metal chelate affinity chromatography (IMAC) and 2D electrophoresis. Dialyze or desalt the sample before performing these procedures. The Protease and Phosphatase Inhibitor formulation is mass spectrometry-compatible because it does not contain AEBSF.

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