Recombinant Carboxypeptidase B is widely used in the biopharmaceutical industry for the removal of C-terminal basic amino acids such as lysine and arginine from proteins and peptides. It plays a critical role in the purification of recombinant therapeutic proteins, ensuring correct C-terminal processing and improving product homogeneity. This enzyme is especially valuable in the production of insulin and other peptide hormones where precise enzymatic processing is required for biological activity.

It is also employed in cell culture processes, particularly in the activation of certain proenzymes or in the cleavage of fusion proteins after affinity chromatography. Due to its high specificity and recombinant origin, it minimizes contamination risks from animal-derived enzymes and supports robust, scalable, and consistent manufacturing processes in GMP environments. Additionally, it is used in analytical workflows for protein characterization, including mass spectrometry, where accurate cleavage is essential for sequencing and post-translational modification analysis.