Recombinant Human Cathepsin D Protein, CF

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Recombinant Human Cathepsin D Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
Measured by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2 (Catalog # ES001). The specific activity is >350 pmol/min/µg, as measured under the described conditions.
Mouse myeloma cell line, NS0-derived human Cathepsin D protein
Leu21-Leu412, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Structure / Form
Pro form
Predicted Molecular Mass
44 kDa
50 kDa, reducing conditions

Product Datasheets

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Supplied as a 0.2 μm filtered solution in MES and NaCl.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

Assay Procedure

  • Assay Buffer: 0.1 M NaOAc, 0.2 M NaCl, pH 3.5
  • Recombinant Human Cathepsin D (rhCathepsin D) (Catalog # 1014-AS)
  • Substrate: MCA-Pro-Leu-Gly-Leu-DPA-Ala-Arg-NH2 (Catalog # ES001), 2 mM stock in DMSO
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Dilute rhCathepsin D to 20 µg/mL in Assay Buffer.
  2. Aliquot 50 µL of 20 µg/mL rhCathepsin D.
  3. Incubate at 37 °C for 30 minutes.
  4. Dilute incubated rhCathepsin D to 1 ng/µL in Assay Buffer.
  5. Dilute Substrate to 60 µM in Assay Buffer.
  6. Load 50 µL of 1 ng/µL rhCathepsin D in a plate, and start the reaction by adding 50 µL of 60 µM Substrate. Include a Substrate Blank containing 50 µL Assay Buffer and 50 µL of 60 µM Substrate.
  7. Read at excitation and emission wavelengths of 320 nm and 405 nm (top read), respectively in kinetic mode for 5 minutes.
  8. 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).

Per Well:
  • rhCathepsin D: 0.050 µg
  • Substrate: 30 µM
Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.


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).

  1. Conner et al. in Handbook of Proteolytic Enzymes Barrett (1998) Academic Press, San Diego, p. 828.
  2. Faust, et al. (1985) Proc. Natl. Acad. Sci. USA 82:4910.
  3. Westley and May (1987) Nucl. Acid Res. 15:3773.
  4. Redecker, et al. (1991) DNA Cell Biol. 10:423.
  5. Rochefort, et al. (2000) Clin. Chim. Acta. 291:157.
  6. Tsukuba, et al. (2000) Mol. Cells 10:601.
Entrez Gene IDs
1509 (Human); 13033 (Mouse)
Alternate Names
cathepsin D (lysosomal aspartyl protease); Cathepsin D; CPSD; CTSD; EC 3.4.23; EC; lysosomal aspartyl peptidase; lysosomal aspartyl protease; MGC2311; neuronal 10

Citations for Recombinant Human Cathepsin D Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

10 Citations: Showing 1 - 10
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  1. A topological refactoring design strategy yields highly stable granulopoietic proteins
    Authors: J Skokowa, B Hernandez, M Coles, M Ritter, M Nasri, J Haaf, N Aghaallaei, Y Xu, P Mir, AC Krahl, KW Rogers, K Maksymenko, B Bajoghli, K Welte, AN Lupas, P Müller, M ElGamacy
    Nature Communications, 2022;13(1):2948.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  2. Intracellular complement C5a/C5aR1 stabilizes beta-catenin to promote colorectal tumorigenesis
    Authors: P Ding, Y Xu, L Li, X Lv, L Li, J Chen, D Zhou, X Wang, Q Wang, W Zhang, T Liao, QH Ji, QY Lei, W Hu
    Cell Reports, 2022;39(9):110851.
    Species: Human
    Sample Types: Recombinant Proteins
    Applications: Bioassay
  3. Global protease activity profiling provides differential diagnosis of pancreatic cysts
    Authors: SL Ivry, JM Sharib, DA Dominguez, N Roy, SE Hatcher, M Yip-Schnei, CM Schmidt, RE Brand, WG Park, M Hebrok, G Kim, AJ O'Donoghue, KS Kirkwood, CS Craik
    Clin. Cancer Res., 2017;0(0):.
    Applications: Bioassay
  4. Oxidation of protein-bound methionine in Photofrin-photodynamic therapy-treated human tumor cells explored by methionine-containing peptide enrichment and quantitative proteomics approach
    Authors: YJ Hsieh, KY Chien, IF Yang, IN Lee, CC Wu, TY Huang, JS Yu
    Sci Rep, 2017;7(1):1370.
    Species: N/A
    Sample Types: Protein
    Applications: Bioassay
  5. The lysosomal protein cathepsin L is a progranulin protease
    Authors: CW Lee, JN Stankowski, J Chew, CN Cook, YW Lam, S Almeida, Y Carlomagno, KF Lau, M Prudencio, FB Gao, M Bogyo, DW Dickson, L Petrucelli
    Mol Neurodegener, 2017;12(1):55.
    Species: Human
    Sample Types: Protein
    Applications: Bioassay
  6. Cleavage of Histone 3 by Cathepsin D in the involuting mammary gland.
    Authors: Khalkhali-Ellis, Zhila, Goossens, William, Margaryan, Naira V, Hendrix, Mary J C
    PLoS ONE, 2014;9(7):e103230.
    Species: Human
    Sample Types: Protein
    Applications: Enzyme Assay
  7. Cathepsin D is partly endocytosed by the LRP1 receptor and inhibits LRP1-regulated intramembrane proteolysis.
    Authors: Derocq D, Prebois C, Beaujouin M, Laurent-Matha V, Pattingre S, Smith GK, Liaudet-Coopman E
    Oncogene, 2012;31(26):3202-12.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  8. Regulation of cathepsin g reduces the activation of proinsulin-reactive T cells from type 1 diabetes patients.
    Authors: Zou F, Schafer N, Palesch D, Brucken R, Beck A, Sienczyk M, Kalbacher H, Sun Z, Boehm BO, Burster T
    PLoS ONE, 2011;6(8):e22815.
    Species: Human
    Sample Types: Protein
    Applications: Enzyme Assay
  9. BACE1 and BACE2 enzymatic activities in Alzheimer's disease.
    Authors: Ahmed RR, Holler CJ, Webb RL
    J. Neurochem., 2010;112(4):1045-53.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Enzyme Assay
  10. Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site. A novel clue for the role of cystatin M/E in epidermal cornification.
    Authors: Cheng T, Hitomi K, van Vlijmen-Willems IM, de Jongh GJ, Yamamoto K, Nishi K, Watts C, Reinheckel T, Schalkwijk J, Zeeuwen PL
    J. Biol. Chem., 2006;281(23):15893-9.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Enzyme Assay


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Recombinant Human Cathepsin D Protein, CF
By Anonymous on 06/17/2019
Application: Immunoassay Standard