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Cathepsin D is a soluble aspartic endopeptidase found in the lysosomes of most mammalian cells. Cathepsin D is activated by proteolytic cleavage of the synthesized inactive zymogen (preproCathepsin D), which is composed of an N-terminal signal peptide, a propeptide, and a catalytic domain. Cathepsin D plays a role in general protein degradation and turnover within the lysosomal compartment, as an important signaling and regulator molecule. Overexpression of Cathepsin D spans across varieties of cancers and is often correlated with poor prognosis. Cathepsin D?s role in pathology is attributed to apoptosis and neurodegeneration.