– The production and breakdown of intracellular proteins is in dynamic equilibrium under stable environmental conditions and when proteins are extracted from cells and tissues in vitro, crude cell extracts contain many endogenous enzymes that are capable of degrading the target proteins, e.g. phosphatases and proteases. These enzymes are released from the cells or activated, leading to the breakdown of the target protein and affecting the results of the analysis. To avoid this, one way to increase the yield of target proteins is to incorporate inhibitors of the relevant enzymes. TargetMol Mass Spectrometry-Compatible Protease Inhibitor Cocktail has a solvent of ddH2O and consists of four components including Aprotinin, Bestatin, E-64 and Leupeptin, which have broad specificity for serine and cysteine proteases and aminopeptidases, and no EDTA. This product is free of AEBSF, which avoids the potential for peak drift in mass spectra. This product does not contain AEBSF, thus avoiding the possible drift of the peaks in the mass spectra. Therefore, protein samples extracted with this product can be used for Mass Spectrometry (MS) detection and analysis, including proteomics. TargetMol Protease Inhibitor Cocktail protects your proteins conveniently and reliably by efficiently inhibiting a wide range of proteases from animal, plant, bacterial, yeast, and fungal samples. It is suitable for extracting proteins from a wide range of tissues and cells to obtain target proteins more efficiently.