Detects human Cathepsin D in Western blots. In Western blots, approximately 20% cross-reactivity with recombinant mouse Cathepsin D is observed, and less than 1% cross-reactivity with recombinant human (rh) Cathepsin A, rhCathepsin B, rhCathepsin C, rhCathepsin L, and rhCathepsin X/Z/P is observed.
Polyclonal Goat IgG
Mouse myeloma cell line NS0-derived recombinant human Cathepsin D Leu21-Leu412 Accession # P07339
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
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
Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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.
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