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Proteases for protein cleavage and protein processing
High-quality proteases like Trypsin and Carboxypeptidase, rec., GMP Grade for biopharmaceutical manufacturing
Streamline your production with our extensive portfolio of proteolytic enzymes. From highly specific cleavage for Active Pharmaceutical Ingredients (API) to general protein degradation, we provide the precision and reliability required for critical raw materials.
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Endoproteases
Trypsin, rec., GMP Grade is expressed in the yeast Pichia pastoris. This procedure in fermentation and enzyme processing eliminates the risk of endotoxins and animal-derived material. No other proteases are used for downstream processing, making this product highly pure, extremely active, and free of any animal-derived material. This makes Trypsin, rec., GMP Grade suited for regulated production environments.
Collagenases
Collagenase I and II are ultrapure, mammalian- and avian-free enzymes dedicated for tissue dissociation. Mild and consistent conditions are essential for high viability and yield of isolated cells. To achieve this, Roche has developed exclusive combinations of our collagenases and neutral proteases offered as Liberase enzyme blends. Customized enzyme combinations are offered on request completing our offering.
Exoproteases
Carboxypeptidase B, rec., GMP Grade expressed in Pichia pastoris is optimal for sensitive manufacturing workflows in biopharma applications, such as active insulin production and post-translational modification of antibodies. Our CpB is animal-component-free and of high performance. Each lot meets narrow quality and activity specifications saving time and money.
Protease inhibitors
Preventing or interrupting protein degradation complements the Roche CustomBiotech protease portfolio in a useful manner. Choose from a variety of different protease inhibitors depending on the protease you need to block.
Download flyer for Trypsin, rec., GMP Grade to discover enyzme quality and reproducibility and how to improve yields while streamlining your processes.