Human Cathepsin D Antibody Summary
Leu21-Leu412
Accession # P07339
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Cathepsin D in U937 Human Cell Line. Cathepsin D was detected in immersion fixed U937 human histiocytic lymphoma cell line using Mouse Anti-Human Cathepsin D Monoclonal Antibody (Catalog # MAB10141) at 8 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red; Catalog # NL007) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Cathepsin D
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).
- Conner et al. in Handbook of Proteolytic Enzymes Barrett (1998) Academic Press, San Diego, p. 828.
- Faust, et al. (1985) Proc. Natl. Acad. Sci. USA 82:4910.
- Westley and May (1987) Nucl. Acid Res. 15:3773.
- Redecker, et al. (1991) DNA Cell Biol. 10:423.
- Rochefort, et al. (2000) Clin. Chim. Acta. 291:157.
- Tsukuba, et al. (2000) Mol. Cells 10:601.
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