Cathepsin-Z exhibits mono- and di-peptidase activity at its C-terminus, unlike cathepsin B, which acts as an endopeptidase . This enzyme is restricted to the cells of the immune system, predominantly monocytes, macrophages, and dendritic cells . It is widely expressed in human tissues, suggesting its involvement in normal intracellular protein degradation across various cell types .
The recombinant form of Cathepsin-Z (Mouse) is typically expressed in HEK293 cells and is purified to a high degree of purity (>95%) as determined by SDS-PAGE . The biological activity of recombinant Cathepsin-Z is measured by its ability to cleave the fluorogenic peptide substrate, Mca-RPPGFSAFK(Dnp)-OH . This specific activity is greater than 1,200 pmoles/min/μg .
Cathepsin-Z is involved in various physiological and pathological processes. It is capable of cleaving regulatory motifs at the C-terminus, affecting the function of targeted molecules . This enzyme may also regulate the maturation of dendritic cells, which is crucial in the initiation of adaptive immunity . Higher levels of Cathepsin-Z are found in tumor and immune cells of prostate and gastric carcinomas, as well as in macrophages of gastric mucosa, especially after infection by Helicobacter pylori . This suggests that Cathepsin-Z may play a role in tumor progression and immune response regulation.