Protease Inhibitor Cocktail, EDTA-Free (100×)

Samples such as cell or tissue extracts contain numerous endogenous proteases and phosphatases, which can readily lead to protein degradation or demodification in the extracts, thereby affecting subsequent protein detection. Therefore, adding appropriate protease and phosphatase inhibitors to extracts and similar samples is an effective method to prevent protein degradation and demodification. This product, Protease Inhibitor Cocktail, EDTA-Free (100×), contains components with broad specificity for aspartic protease, cysteine protease, serine protease, acidic protease, and aminopeptidase, including AEBSF, Aprotinin, Bestatin, E-64 (trans-Epoxysuccinyl-L-leucylamido-(4-guanidino)butane), Leupeptin, and Pepstatin A.

AEBSF is a water-soluble irreversible inhibitor of serine proteases, with inhibition constants similar to those of PMSF and DFP. It effectively inhibits proteases such as trypsin, chymotrypsin, plasmin, kallikrein, and thrombin, serving as a substitute for PMSF and DFP. AEBSF exhibits lower toxicity, better water solubility, and superior stability in aqueous solutions. Aprotinin is a competitive reversible inhibitor of serine proteases; Bestatin is a reversible inhibitor of aminopeptidases; E-64 is an irreversible inhibitor of cysteine proteases; Leupeptin is a reversible inhibitor of serine and cysteine proteases; and Pepstatin A is a reversible inhibitor of aspartic proteases.