Detection of Human Cathepsin D by Western Blot. Western blot shows lysates of PANC‑1 human pancreatic carcinoma cell line and MCF‑7 human breast cancer cell line. PVDF membrane was probed with 0.2 µg/mL of Mouse Anti-Human Cathepsin D Monoclonal Antibody |
(Catalog # MAB1014) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). Specific bands were detected for Cathepsin D at approximately 28 and 46 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Cathepsin D is a lysosomal aspartic protease of the pepsin family (1). Human cathepsin D is synthesized as a precursor protein, consisting of a signal peptide (aa 1‑18), a propeptide (aa 19-64), and a mature chain (aa 65‑412) (2‑4). The mature chain can be processed further to the light (aa 65‑161) and heavy (aa 169‑412) chains. It is expressed in most cells and overexpressed in breast cancer cells (5). It is a major enzyme in protein degradation in lysosomes, and also involved in the presentation of antigenic peptides. Mice deficient in this enzyme showed a progressive atrophy of the intestinal mucosa, a massive destruction of lymphoid organs, and a profound neuronal ceroid lipofucinosis, indicating that cathepsin D is essential for proteolysis of proteins regulating cell growth and tissue homeostasis (6). Cathepsin D secreted from human prostate carcinoma cells are responsible for the generation of angiostatin, a potent endogeneous inhibitor of angiogenesis (6).
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