Analytical Data
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Gene name
Cathepsin C/DPPI
- Application
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Alternative Names
CTS-C; DPPI; CPPI; DPP1; DPP-I; HMS; JP; JPD; PALS; PLS; Dipeptidyl Peptidase I; Dipeptidyl transferase; Cathepsin J
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P97821
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Expression Region
Pro231~Leu462
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Molecular Weight
26kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Cathepsin C, also known as dipeptidyl peptidase I (DPPI), is a lysosomal cysteine protease that plays a crucial role in the activation of various proenzymes, particularly those involved in the immune response and inflammation. Mutations in the gene encoding Cathepsin C are associated with several hereditary diseases, including Papillon-Lefèvre syndrome and hypohidrotic ectodermal dysplasia. These conditions highlight the importance of Cathepsin C in normal physiological processes and its potential as a therapeutic target. The study and characterization of recombinant Cathepsin C/DPPI have gained significant traction as researchers aim to understand its biochemical properties, substrate specificity, and role in various pathological conditions. By producing recombinant forms of the protein, scientists can conduct functional assays to investigate its enzymatic activity and interactions with inhibitors or substrates. This research not only enhances our understanding of Cathepsin C's biological functions but also opens avenues for developing targeted therapies for disorders linked to its dysfunction. The recombinant protein serves as a valuable tool for drug discovery and the development of novel therapeutic strategies aimed at modulating immune responses and inflammatory processes.
