Recombinant Rat Cathepsin C/DPPI Protein, CF

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R&D Systems Recombinant Proteins and Enzymes
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Product Details

Recombinant Rat Cathepsin C/DPPI Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane
Endotoxin Level
<0.1 EU per 1 μg of the protein by the LAL method.
Measured by its ability to cleave the fluorogenic peptide substrate, Gly-Arg-7-amido-4-methylcoumarin (GR-AMC). The specific activity is >25,000 pmol/min/μg, as measured under the described conditions.
Mouse myeloma cell line, NS0-derived rat Cathepsin C/DPPI protein
Asp25-Leu462, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Structure / Form
Pro form
Predicted Molecular Mass
51 kDa
56-62 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

  • Activation Buffer: 25 mM MES, 5 mM DTT, pH 5.5
  • Assay Buffer: 25 mM MES, 50 mM NaCl, 5 mM DTT, pH 6.0
  • Recombinant Rat Cathepsin C/DPPI (rrCathepsin C) (Catalog # 8285-CY)
  • Recombinant Human Cathepsin L (rhCathepsin L) (Catalog # 952-CY)
  • Substrate: Gly-Arg-AMC (Bachem, Catalog # I-1215)
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Dilute rrCathepsin C to 20 µg/mL in Activation Buffer.
  2. Dilute rhCathepsin L to 2 µg/mL in Activation Buffer.
  3. Combine equal volumes of diluted rrCathepsin C and diluted rhCathepsin L for final concentrations of 10 µg/mL and 1 µg/mL respectively.
  4. Incubate at room temperature for 30 minutes to activate rrCathepsin C.
  5. Dilute activated rrCathepsin C to 0.02 µg/mL in Assay Buffer.
  6. Dilute Substrate to 100 µM in Assay Buffer.
  7. Load 50 µL of the 0.02 µg/mL rrCathepsin C into a plate, and start the reaction by adding 50 µL of 100 µM Substrate.  Include a Substrate Blank containing 50 µL Assay Buffer and 50 µL of 100 µM Substrate.
  8. Read at excitation and emission wavelengths of 380 nm and 460 nm (top read), respectively, in kinetic mode for 5 minutes.
  9. 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 7-amino, 4-Methyl Coumarin (Sigma, Catalog # A-9891).

Per Well:
  • rrCathepsin C: 0.001 µg
  • Substrate: 50 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 C/DPPI

Cathepsin C (CTSC), also known as dipeptidyl-peptidase I (DPPI), is a chloride-dependent cysteine protease in the papain family (1-3). It sequentially removes dipeptides from the free N-terminus of proteins and peptides. It has broad specificity except that it does not cleave proteins with a basic amino acid (Arg or Lys) in the N-terminal position or with a proline on either side of the scissile bond. Cathepsin C is synthesized with a large propeptide followed by a mature region, which is further cleaved into heavy and light chains during processing. The N-terminal region of the propeptide is known as the exclusion domain. It is present in the mature, active enzyme and regulates access of substrates to the active site (4). Cathepsin C is widely expressed and plays a major role in lysosomal degradation and enzyme activation. It activates granule serine proteases in cytotoxic T lymphocytes and natural killer cells (Granzymes A and B), mast cells (Tryptase and Chymase), and neutrophils (Cathepsin G and Elastase) by removing their N-terminal activation dipeptides (5).

  1. Turk, B.E. et al. (2004) in Handbook of Proteolytic Enzymes (ed. Barrett, A.J. et al.) pp. 1192, Elsevier Academic Press, San Diego.
  2. Minarowska, A. et al. (2012) Folia Histochem. Cytobiol. 50:20.
  3. Ishidoh, K. et al. (1991) J. Biol. Chem. 266:16312.
  4. Turk, D. et al. (2001) EMBO J. 20:6570.
  5. Dahl, S.W. et al. (2001) Biochemistry 40:1671.
Entrez Gene IDs
1075 (Human); 13032 (Mouse); 25423 (Rat)
Alternate Names
Cathepsin C; cathepsin CEC; Cathepsin J; CPPIHMS; CTSC; dipeptidyl peptidase 1; Dipeptidyl peptidase I; Dipeptidyl transferase; dipeptidyl-peptidase I; DPP1; DPPI; DPP-I; JP; JPD; PALS; PLS


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