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AB158099

Recombinant Human Cathepsin C protein (GST tag N-Terminus)

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Recombinant Human Cathepsin C protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 463 aa range, expressed in Wheat germ, suitable for ELISA, WB.

View Alternative Names

CPPI, CTSC, Dipeptidyl peptidase 1, Cathepsin C, Cathepsin J, Dipeptidyl peptidase I, Dipeptidyl transferase, DPP-I, DPPI

1 Images
SDS-PAGE - Recombinant Human Cathepsin C protein (AB158099)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human Cathepsin C protein (AB158099)

ab158099 on a 12.5% SDS-PAGE stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

WB, ELISA

applications

Biologically active

No

Accession

P53634

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.31% Glutathione

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

This product was previously labelled as DPP1.
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Sequence info

[{"sequence":"MGAGPSLLLAALLLLLSGDGAVRCDTPANCTYLDLLGTWVFQVGSSGSQRDVNCSVMGPQEKKVVVYLQKLDTAYDDLGNSGHFTIIYNQGFEIVLNDYKWFAFFKYKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKKVGTASENVYVNTAHLKNSQEKYSNRLYKYDHNFVKAINAIQKSWTATTYMEYETLTLGDMIRRSGGHSRKIPRPKPAPLTAEIQQKILHLPTSWDWRNVHGINFVSPVRNQASCGSCYSFASMGMLEARIRILTNNSQTPILSPQEVVSCSQYAQGCEGGFPYLIAGKYAQDFGLVEEACFPYTGTDSPCKMKEDCFRYYSSEYHYVGGFYGGCNEALMKLELVHHGPMAVAFEVYDDFLHYKKGIYHHTGLRDPFNPFELTNHAVLLVGYGTDSASGMDYWIVKNSWGTGWGENGYFRIRRGTDECAIESIAVAATPIPKL","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":463,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"P53634","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

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.
Biological function summary

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.

Pathways

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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Specifications

Form

Liquid

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General info

Function

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).

Sequence similarities

Belongs to the peptidase C1 family.

Post-translational modifications

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.. In approximately 50% of the complexes the exclusion domain is cleaved at position 58 or 61. The two parts of the exclusion domain are held together by a disulfide bond.

Subcellular localisation

Lysosome

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Product protocols

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Target data

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).
See full target information CTSC
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