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

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.

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.

Reconstitution Calculator

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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).

Item	Value
References	Turk, B. et al. (2004) in Handbook of Proteolytic Enzymes (ed. Barrett, A.J. et al.) p. 1192, Academic Press, San Diego. Dahl, S.W. et al. (2001) Biochemistry 40:1671. Toomes, A.J. et al. (1999) Nat. Genet. 23:421.
Entrez Gene IDs	1075 (Human); 13032 (Mouse); 25423 (Rat)
Alternate Names	CPPIHMS, CTSC, Cathepsin C, Cathepsin J, DPP-I, DPP1, DPPI, Dipeptidyl peptidase I, Dipeptidyl transferase, JP, JPD, PALS, PLS, cathepsin CEC 3.4.14.1, dipeptidyl peptidase 1, dipeptidyl-peptidase I

Citations for Recombinant Human Cathepsin C/DPPI Protein, CF (7)

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Citations are publications that use Bio-Techne products. Selected citations for Recombinant Human Cathepsin C/DPPI Protein, CF include:

Species: Human
Sample Types: Whole Cells
Applications: Bioassay

P Cheung et al. (2021), Repression of CTSG, ELANE and PRTN3-mediated histone H3 proteolytic cleavage promotes monocyte-to-macrophage differentiation Nature Immunology, 22(6):711-722.
PMID: 34017121
Species: Human
Sample Types: Protein
Applications: Bioassay

S Kim et al. (2021), Decursin inhibits cell growth and autophagic flux in gastric cancer via suppression of cathepsin C American journal of cancer research, 11(4):1304-1320.
PMID: 33948359
Species: N/A
Sample Types: Recombinant Protein
Applications: Bioassay

JB Schaal et al. (2017), Suppression and resolution of autoimmune arthritis by rhesus ?-defensin-1, an immunomodulatory macrocyclic peptide PLoS ONE, 12(11):e0187868.
PMID: 29145473
Species: N/A
Sample Types: Fluorogenic Peptide Substrate
Applications: Enzyme Assay

Hamilton G et al. (2008), Cystatin F is a cathepsin C-directed protease inhibitor regulated by proteolysis. EMBO J., 27(3):499-508.
PMID: 18256700
Species: Human
Sample Types: Cell Lysates
Applications: Enzyme Assay

Burster T et al. (2007), Design of protease-resistant myelin basic protein-derived peptides by cleavage site directed amino acid substitutions. Biochem. Pharmacol., 74(10):1514-23.
PMID: 17803968
Species: N/A
Sample Types: Fluorogenic Peptide Substrate
Applications: Enzyme Assay

Methot N et al. (2007), Inhibition of the activation of multiple serine proteases with a cathepsin C inhibitor requires sustained exposure to prevent pro-enzyme processing. J. Biol. Chem., 282(29):20836-46.
PMID: 17535802
Species: Human
Sample Types: Recombinant Protein
Applications: Enzyme Assay

Falgueyret JP et al. (2004), An activity-based probe for the determination of cysteine cathepsin protease activities in whole cells. Anal. Biochem., 335(2):218-27.
PMID: 15556560

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Recombinant Human Cathepsin C/DPPI Protein, CF

Name: Anonymous

Application: Binding assay/Protein-protein interaction

Reason for Rating: While Cathepsin did activate ms Neutrophil elastase Cat No. 4517-SE-010 the amount of total protein activated was less. The Activity assay of NE after cathepsin activation was not at 100% compared to a control hu NE sample.

Verified Customer | Posted 06/24/2016

I ran the activity assay at greater than 1ng/mL.

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Recombinant Human Cathepsin C/DPPI Protein, CF

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