Recombinant Human Cathepsin Z protein (denatured) (His tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Cathepsin Z also known as cathepsin X or CTSZ is a lysosomal cysteine protease with a molecular weight of approximately 34 kDa. It is expressed mainly in immune cells such as macrophages and dendritic cells but also found in other tissues including liver kidney and spleen. This protease performs proteolytic functions which involve cleaving peptide bonds in proteins contributing to protein catabolism in cells. The widespread expression of Cathepsin Z suggests its involvement in various physiological processes.

Biological function summary

Cathepsin Z participates in immune response regulation and cellular adhesion processes. It belongs to the papain-like cysteine protease family. Notably it associates with integrins to influence cell-extracellular matrix interactions affecting cell migration and adhesion. By modulating these processes Cathepsin Z impacts immune surveillance and tissue remodeling demonstrating its multifaceted role in maintaining cellular homeostasis.

Pathways

Cathepsin Z engages significantly in apoptotic and antigen-presenting pathways. In apoptosis it influences cell death by degrading specific substrates involved in cell survival. It also assists in the processing of antigens within dendritic cells facilitating effective antigen presentation to T cells. Related proteins such as Cathepsin S and Cathepsin L which also partake in lysosomal pathways further illustrate the shared functionality and redundancy within this protease family enabling a robust regulatory network.

Cathepsin Z has implications in cancer progression and neurodegenerative diseases. It is often overexpressed in cancerous tissues where it aids tumor cell invasion and metastasis through degradation of extracellular components. Additionally alterations in Cathepsin Z activity are linked to Alzheimer's disease where it may affect the processing of amyloid precursor proteins similar to its interaction with other proteins like Cathepsin B. These connections highlight the potential for Cathepsin Z as a target for therapeutic intervention in various pathological conditions.