Cathepsin Z (CTSZ), a member of the cysteine cathepsin protease family, is a lysosomal enzyme involved in protein degradation, extracellular matrix remodeling, and antigen processing. Unlike other cathepsins, CTSZ uniquely combines a protease domain with a conserved integrin-binding RGD motif, enabling interactions with cell surface receptors and extracellular signaling. It is expressed in immune cells (e.g., macrophages, dendritic cells) and tissues like the liver, kidney, and placenta. CTSZ plays roles in inflammation, angiogenesis, and tumor progression, with dysregulation linked to cancers, autoimmune diseases, and neurodegenerative disorders.
CTSZ antibodies are essential tools for studying its expression, localization, and function. They enable detection via Western blotting, immunohistochemistry, and flow cytometry, aiding research into CTSZ's role in disease mechanisms. For example, elevated CTSZ levels correlate with tumor invasiveness and poor prognosis in certain cancers, while reduced activity is implicated in rheumatoid arthritis. Antibodies targeting the RGD motif also explore its integrin-mediated signaling pathways. Additionally, structural studies using CTSZ antibodies contribute to drug development, particularly for inhibitors designed to modulate its proteolytic activity in pathological conditions. These antibodies thus serve as critical reagents in both basic research and therapeutic exploration.