Recombinant Human Cathepsin C/CTSC/DPPI Protein (His Tag) (PKSH031574)
For research use only.
| Synonyms | CPPI, DPP-I, DPP1, DPPI, HMS, JP, JPD, PALS, PDON1, PLS |
| Species | Human |
| Expression Host | HEK293 Cells |
| Sequence | Met 1-Leu 463 |
| Accession | NP_001805.3 |
| Calculated Molecular Weight | 51.0 kDa |
| Observed Molecular Weight | 55 kDa |
| Tag | C-His |
| Bio-activity | Measured by its ability to cleave the fluorogenic peptide substrate, Gly-Arg-7-amido-4-methylcoumarin (GRAMC). The specific activity is > 200 pmoles/min/μg. (Activation description: The proenzyme needs to be activated by Cathepsin L for an activated form) |
| Purity | > 92 % as determined by reducing SDS-PAGE. |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
| Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
| Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
| Formulation |
Lyophilized from sterile PBS, pH 7.4 Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
| Reconstitution | Please refer to the printed manual for detailed information. |
| Background | Cathepsins are proteases found in many types of cells conserved in all animals, which have a vital role in mammalian cellular turnover such as bone resorption. The lysosomal cysteine protease Cathepsin C (CTSC), also known as dipeptidyl peptidase I (DPPI/DPP1), activates a number of granule-associated serine proteases with pro-inflammatory and immune functions by removal of their inhibitory N-terminal dipeptides. This lysosomal exo-cysteine protease belonging to the peptidase C1 family. Active cathepsin C is found in lysosomes as a 200-kDa multimeric enzyme. Subunits constituting this assembly all arise from the proteolytic cleavage of a single precursor giving rise to three peptides: the propeptide, the alpha- and the beta-chains. It is a central coordinator for activation of many serine proteases in immune/inflammatory cells. Defects in the Cathepsin C have been shown to be a cause of Papillon-Lefevre disease, an autosomal recessive disorder characterized by palmoplantar keratosis and periodontitis. Cathepsin C plays a key role in the activation of several degradative enzymes linked to tissue destruction in inflammatory diseases. Thus, it is a therapeutic target for the treatment of a number of inflammatory and autoimmune diseases. |
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