Anti-Cathepsin D Rabbit mAb [12B24]

Protein A affinity purification

Cathepsin-D

Cathepsin D is a member of aspartic protease family and performs lysosomal proteolytic processing functions. It is synthesized as inactive pro-Cathepsin D zymogen, delivered to lysosomes and proteolytically activated under acidic lysosomal condition to degrade aged intracellular proteins and endocytosed exogenous substrates. Beyond lysosomal compartment, Cathepsin D can be secreted into extracellular matrix to drive matrix remodeling and apoptosis regulation. Upregulated Cathepsin D is frequently observed in breast, ovarian and multiple cancers; it degrades basement membrane components to facilitate tumor invasion and metastasis, and participates in tumor microenvironment modulation, autophagy and cellular stress response. Its expression serves as a potential prognostic biomarker for certain malignancies and is widely investigated in tumor pathology and lysosome biology.

Lysosome