Widely used in cell culture and tissue dissociation, this enzyme selectively cleaves peptide bonds at the carboxyl side of aromatic amino acids like tyrosine, phenylalanine, and tryptophan. It is particularly useful in the detachment of cells during subculturing, especially when working with delicate tissues or primary cell lines where gentle dissociation is required.

Due to the TLCK treatment, the preparation is free from trypsin-like activity, reducing unwanted proteolytic side reactions and improving specificity. This makes it ideal for applications requiring high precision, such as protein sequencing and limited proteolysis studies.

It is also employed in the pharmaceutical industry for the production of therapeutic proteins and in research settings for zymogen activation and enzyme mechanism studies. Its high specificity and controlled activity support reproducible results in enzymatic digestion protocols.