Skip to main content

Recombinant Human Cathepsin C/DPPI Protein, CF

Bio-Techne includes R&D Systems | Catalog # 1071-CY

Catalog #
Availability
Size / Price
Qty
Loading...
1071-CY-010

Key Product Details

Source

NS0

Accession #

Structure / Form

Pro form

Conjugate

Unconjugated

Applications

Enzyme Activity

Product Specifications

Source

Mouse myeloma cell line, NS0-derived human Cathepsin C/DPPI protein
Asp25-Leu463, with a C-terminal 10-His tag

Purity

>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.

N-terminal Sequence Analysis

Asp25

Predicted Molecular Mass

51 kDa

SDS-PAGE

60 kDa, reducing conditions

Activity

Measured by its ability to cleave the fluorogenic peptide substrate, Gly-Arg-7-amido-4-methylcoumarin (GR-AMC).
The specific activity is >200 pmol/min/µg, as measured under the described conditions.

Formulation, Preparation and Storage

1071-CY
Formulation Supplied as a 0.2 μm filtered solution in MES and NaCl.
Shipping The product is shipped with dry ice or equivalent. 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.

Background: Cathepsin C/DPPI

Cathepsin C, also known as dipeptidyl-peptidase I (DPPI), is a cysteine protease of the papain family (1). Cathepsin C sequentially removes dipeptides from the free N-termini of proteins and peptides. It has broad specificity except that it does not cleave a basic amino acid (Arg or Lys) in the N-terminal position or Pro on either side of the scissle bond. It requires halide ions for activity. The pro form contains a pro peptide and a catalytic region, which can be further processed into heavy/ alpha and light/ beta chains that are linked by a disulfide bond. It is broadly distributed. Cathepsin C plays a role in the lysosomal degradation. It also functions as a key enzyme in the activation of 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 (2). Loss of function mutations in the Cathepsin C gene result in periodontal disease and palmoplantar keratosis (3).

References

  1. Turk, B. et al. (2004) in Handbook of Proteolytic Enzymes (ed. Barrett, A.J. et al.) p. 1192, Academic Press, San Diego.
  2. Dahl, S.W. et al. (2001) Biochemistry 40:1671.
  3. Toomes, A.J. et al. (1999) Nat. Genet. 23:421.

Alternate Names

CTSC, DPPI, PALS, PLS

Entrez Gene IDs

1075 (Human); 13032 (Mouse); 25423 (Rat)

Gene Symbol

CTSC

UniProt

Additional Cathepsin C/DPPI Products

Product Documents for Recombinant Human Cathepsin C/DPPI Protein, CF

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human Cathepsin C/DPPI Protein, CF

For research use only

Loading...
Loading...