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Cathepsin D, an enzyme that degrades proteins, was originally cloned during the search of estrogen responsive genes in MCF-7 cells. Cathepsin D is synthesized as the 43kDa preprocathepsin D that is cleaved to form a 46kDa glycosylated procathepsin D. Procathepsin is then processed into a 44kDa active Cathepsin D. The active and mature forms undergo a further cleavage that yields 28kDa and 15kDa (heavy and light chains, respectively) fragments in SDS-PAGE. The heavy and light chains of Cathepsin D are released into the extracellular medium. The maturation process of Cathepsin D occurs through the transit from the endoplasmic reticulum, Golgi apparatus, and to the lysosomes. Estrogens stimulate cell proliferation in a number of tumor cell lines and anti-estrogen therapy is often used in the treatment of breast cancer patients. Therefore, Cathepsin D, which is estrogen inducible, may have a role during the pathogenesis of breast tumors. Additionally, several other roles have been proposed for this enzyme, such as tissue remodeling, tumor invasion, and embryo implantation.Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting
