Human Cathepsin D Biotinylated Antibody Summary
Accession # P07339
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.
Cathepsin D in Human Lung. Cathepsin D was detected in immersion fixed paraffin-embedded sections of human lung array using Goat Anti-Human Cathepsin D Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF1014) at 15 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). Lower panel shows a lack of labeling if primary antibodies are omitted and tissue is stained only with secondary antibody followed by incubation with detection reagents. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.
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 (residues 1‑18), a propeptide (residues 19-64), and a mature chain (residues 65‑412) (2‑4). The mature chain can be processed further to the light (residues 65‑161) and heavy (residues 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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