Proteases (or peptidases) are proteolytic enzymes that hydrolyze the peptide bonds between amino acids. Endoproteases are proteases that cleave intramolecular linkages within proteins, making these types of enzymes important tools for industrial processes and biochemical research. TEV Protease and Thrombin are examples of endoproteases that target well-defined consensus sequences, a property which makes them useful for removing affinity tags and for cleaving fusion proteins. In contrast, promiscuous proteases such as trypsin cut peptides more frequently. Trypsin targets peptide bonds adjacent to lysine and arginine residues, enabling researchers to digest proteins into discriminate fragments in preparation for following steps such as peptide mapping.
Endoproteases are also critical for cleaving amino acid linkages to interconvert prodrugs to their parental drugs. For example, Trypsin and Lysyl-Endopeptidase (Lys-c) are involved in removal of the C-peptide from pro-insulin, a necessary step towards the production of insulin.
To facilitate production processes that require large-scale proteolysis steps, Immobilized Proteases offer several advantages, which include:
• Cost Savings – the immobilized enzyme resin can be reused up to 20 times
• Protocol Flexibility – immobilized proteases are amenable to suspension or in-column digestion protocols
• Higher Product Yield and Quality – enzyme separation steps are eliminated
SignalChem’s Protease Enzymes are fully characterized for their activity and specificity. All products, including agarose and/or silica cross-linked proteases, are available in microgram to gram quantities.