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 in Human Prostate Cancer Tissue. Cathepsin D was detected in immersion fixed paraffin-embedded sections of human prostate cancer tissue using Mouse Anti-Human Cathepsin D Monoclonal Antibody (Catalog # MAB1014) at 5 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Mouse IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC001). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to epithelial cell cytoplasm. View our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents.|
|Detection of Human Cathepsin D by Simple WesternTM. Simple Western lane view shows lysates of PANC‑1 human pancreatic carcinoma cell line and MCF‑7 human breast cancer cell line, loaded at 0.2 mg/mL. Specific bands were detected for Cathepsin D at approximately 36 and 52‑57 kDa (as indicated) using 2 µg/mL of Mouse Anti-Human Cathepsin D Monoclonal Antibody (Catalog # MAB1014). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.|
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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