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Life Science > Metabolomics > Enzyme Explorer > Learning Center > Protease Inhibitors |
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Overview of Proteolytic Activities and Inhibition Strategies Broad-Spectrum Inhibitors of Proteolytic Enzyme Classes Broad-Spectrum Protease Inhibitor Cocktails Protease Inhibitor Cocktail Products Protease Inhibitor Panel (INHIB-1) (PDF 88 kb) Recombinant Protein Expression Extraction and Stabilization Guide (PDF 268 kb) Proteolytic hydrolysis of peptide bonds was first studied as a function of digestion in higher animals. It is now recognized as an essential and ubiquitous mechanism for the regulation of a myriad of physiological processes. Inhibition of proteolytic activity is generally employed for two purposes:
Four main classes of proteolytic enzymes have been routinely utilized to describe proteases. The serine proteases are probably the best characterized. This class of proteases includes trypsin, chymotrypsin and elastase. The cysteine protease class includes papain, calpain and lysosomal cathepsins. Aspartic proteases include pepsin and rennin. Metallo-proteases include thermolysin and carboxypeptidase A. During isolation and characterization, one or all four classes of proteases may pose a threat to the fate of a protein. Broad spectrum protease inhibitors and mixtures, or Cocktails, have been developed to help protect the integrity of proteins. Sigma offers and manufactures the broadest range of protease inhibitors and inhibitor cocktails of any supplier. Sigma Inhibitor Cocktails have been specifically formulated for particular applications as they relate to the biological source or method of expression. The Sigma Protease Inhitior Panel (PDF 88 kb) allows you to design an individualized inhibition strategy and shows you how to formulate your cocktails. |
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