Recombinant Human Cathepsin C protein is a Human Full Length protein, in the 1 to 463 aa range, expressed in Wheat germ and suitable for ELISA, WB.
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Application | Reactivity | Dilution info | Notes |
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Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
Thiol protease (PubMed:1586157). Has dipeptidylpeptidase activity (PubMed:1586157). Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids (PubMed:1586157). Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate (PubMed:1586157). Can act as both an exopeptidase and endopeptidase (PubMed:1586157). Activates serine proteases such as elastase, cathepsin G and granzymes A and B (PubMed:8428921).
CPPI, CTSC, Dipeptidyl peptidase 1, Cathepsin C, Cathepsin J, Dipeptidyl peptidase I, Dipeptidyl transferase, DPP-I, DPPI
Recombinant Human Cathepsin C protein is a Human Full Length protein, in the 1 to 463 aa range, expressed in Wheat germ and suitable for ELISA, WB.
pH: 8
Constituents: 0.79% Tris HCl, 0.31% Glutathione
Thiol protease (PubMed:1586157). Has dipeptidylpeptidase activity (PubMed:1586157). Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids (PubMed:1586157). Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate (PubMed:1586157). Can act as both an exopeptidase and endopeptidase (PubMed:1586157). Activates serine proteases such as elastase, cathepsin G and granzymes A and B (PubMed:8428921).
Belongs to the peptidase C1 family.
N-glycosylated. While glycosylation at Asn-53, Asn-119 and Asn-276 is mediated by STT3A-containing complexes, glycosylation at Asn-29 is mediated STT3B-containing complexes.
This product was previously labelled as DPP1.
Cathepsin C also known as dipeptidyl peptidase I is a lysosomal cysteine protease with a molecular mass of approximately 51 kDa. It functions mechanically by cleaving off dipeptides from the N-terminal end of proteins and peptides. Cathepsin C is widely expressed in various tissues with higher levels in immune cells like neutrophils and macrophages. This enzyme activates serine proteases from their inactive zymogen forms which is important for immune responses.
The enzyme contributes significantly to the immune system. It forms part of a multi-enzyme complex that processes proenzymes such as granzymes and cathepsin G into their active forms. Through these actions Cathepsin C regulates cellular activities linked to inflammation and apoptosis. The proteolytic activity it provides is critical for the functioning of immune-related cells facilitating defense mechanisms against pathogens.
Cathepsin C plays roles in the inflammatory and immune response pathways. It connects to the granzyme and lysosomal pathways important in processing and regulating granzyme activities critical for cytotoxic T lymphocyte functions. Cathepsin C maintains connections with proteins like granzymes and cathepsin G each involved in mediating immune responses and cellular death.
Cathepsin C is associated with conditions such as Papillon-Lefèvre Syndrome and aggressive periodontitis. These disorders arise due to disruptions in immune protection resulting from mutations in the Cathepsin C gene. The enzyme's abnormal activity in these diseases highlights its connection with proteins such as neutrophil elastase which play critical roles in tissue degradation processes leading to periodontal disease.
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ab158099 on a 12.5% SDS-PAGE stained with Coomassie Blue.
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