Description
Cathepsin D, also known as lysosomal aspartyl protease, is a member of the peptidase C1 family, which is a normal and major component of lysosomes, and is found in almost all cells and tissues of mammals. The main physiological functions of cathepsin D consist of metabolic degradation of intracellular proteins, activation and degradation of polypeptide hormones and growth factors, activation of enzymatic precursors, processing of enzyme activators and inhibitors, brain antigen processing and regulation of programmed cell death. In addition, it secreted from human prostate carcinoma cells are responsible for the generation of angiostatin, a potent endogenous inhibitor of angiogenesis, suggesting its contribution to the prevention of tumor growth and angiogenesis-dependent growth of metastases. Recombinant human Cathepsin D, fused to His-tag at C-terminus, was expressed in HEK293 cell and purified by using conventional chromatography techniques