Anti-Cathepsin D Antibody

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Cathepsin D is a normal lysosomal protease that is expressed in all cells. It is an aspartyl protease with a pH optimum in the range of 3-5, and contains two N-linked oligosaccharides. Cathepsin D is synthesized as an inactive 52 kDa pro-enzyme. Activation involves the proteolytic removal of the 43 amino acid profragment and an internal cleavage to generate the two-chain form made up of 34 and 14 kDa subunits. Cathepsin D contains the mannose-6-phosphate lysosomal localization signal that targets the enzyme to the lysosomal compartment where it functions in the normal degradation of proteins. In certain tumor cells, Cathepsin D is abnormally processed and is secreted in its 52 kDa precursor form. Numerous clinical studies as well as in vitro evidence sµggest that cathepsin D plays an important role in malignant transformation and may be a useful prognostic indicator for breast cancer.