>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
<1.0 EU per 1 μg of the protein by the LAL method.
44 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
Dilute rmCathepsin D to 20 µg/mL in Assay Buffer.
Incubate at RT for 10 minutes.
Dilute activated rmCathepsin D to 0.4 ng/µL in Assay Buffer.
Dilute Substrate to 20 µM in Assay Buffer.
Load 50 µL of the 0.4 ng/µL rmCathepsin D in a plate, and start the reaction by adding 50 µL of 20 µM Substrate. Include a Substrate Blank containing 50 µL Assay Buffer and 50 µL of 20 µM Substrate.
Read at excitation and emission wavelengths of 320 nm and 405 nm (top read), respectively in kinetic mode for 5 minutes.
Calculate specific activity:
Specific Activity (pmol/min/µg) =
Adjusted Vmax* (RFU/min) x Conversion Factor** (pmol/RFU)
amount of enzyme (µg)
*Adjusted for Substrate Blank **Derived using calibration standard MCA-Pro-Leu-OH (Bachem, Catalog # M-1975)
rmCathepsin D: 0.020 µg
Substrate: 10 µM
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Cathepsin D Protein, CF
cathepsin D (lysosomal aspartyl protease)
lysosomal aspartyl peptidase
lysosomal aspartyl protease
Cathepsin D is a lysosomal aspartic protease of the pepsin family (4). Mouse Cathepsin D is synthesized as a precursor protein, consisting of a signal peptide (residues 1‑20), a propeptide (residues 21‑64), and a mature chain (residues 65‑410) (1‑3). 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 is responsible for the generation of angiostatin, a potent endogeneous inhibitor of angiogenesis (6).
Diedrich, et al. (1990) Nucl. Acid Res. 18:7184.
Grusby, et al. (1990) Nucl. Acid Res. 18:4008.
Hetman, et al. (1994) DNA Cell Biol. 13:419.
Conner (2004) in Handbook of Proteolytic Enzymes (Barrett, et al. eds) Elsevier Academic Press, San Diego, p. 43.
Rochefort, et al. (2000) Clin. Chim. Acta. 291:157.
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Bio-Techne appreciates the critical role that you and our products and services play in research efforts to further scientific innovation and discovery. We are continually assessing our manufacturing and supplier capabilities during the COVID-19 situation and are implementing precautionary measures to ensure uninterrupted supply of products and services. Currently, and as we abide by local shelter in place orders across the world, we are fully operational and do not anticipate any material supply disruptions across our Bio-Techne brands and product lines. As the situation evolves, our goal is to utilize preventive measures to reduce the threat that COVID-19 poses to our ability to meet the needs of our customers globally.