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AB276277

Recombinant Human Cathepsin C protein (His tag)

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Recombinant Human Cathepsin C protein (His tag) is a Human Full Length protein, in the 1 to 463 aa range, expressed in HEK 293 cells, with >92%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE.

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 (His tag) (AB276277)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human Cathepsin C protein (His tag) (AB276277)

SDS-PAGE analysis of ab276277

Key facts

Purity

>92% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

HEK 293 cells

Tags

His tag C-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P53634

Animal free

No

Carrier free

Yes

Species

Human

Storage buffer

pH: 7.4 Constituents: PBS

storage-buffer

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Complementary Products

Primary Antibodies

AB314644

Anti-Cathepsin C antibody [EPR26636-76]

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Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Cathepsin C antibody [EPR26636-76] (AB314644)

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Proteins & Peptides

AB153798

Recombinant Human PR3 protein

SDS-PAGE - Recombinant Human PR3 protein (AB153798)

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Proteins & Peptides

AB307481

Recombinant Human Granzyme B Protein (His tag)

Mass Spectrometry - Recombinant Human Granzyme B Protein (His tag) (AB307481)

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Primary Antibodies

AB303516

Anti-Hsp 90 alpha antibody [EPR27270-11]

BOND RX™ Validated|20ul selling size|RabMAb|Recombinant|KO Validated|Trial Size

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Hsp 90 alpha antibody [EPR27270-11] (AB303516)

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  • 0
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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MGAGPSLLLAALLLLLSGDGAVRCDTPANCTYLDLLGTWVFQVGSSGSQRDVNCSVMGPQEKKVVVYLQKLDTAYDDLGNSGHFTIIYNQGFEIVLNDYKWFAFFKYKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKKVGTASENVYVNIAHLKNSQEKYSNRLYKYDHNFVKAINAIQKSWTATTYMEYETLTLGDMIRRSGGHSRKIPRPKPAPLTAEIQQKILHLPTSWDWRNVHGINFVSPVRNQASCGSCYSFASMGMLEARIRILTNNSQTPILSPQEVVSCSQYAQGCEGGFPYLIAGKYAQDFGLVEEACFPYTGTDSPCKMKEDCFRYYSSEYHYVGGFYGGCNEALMKLELVHHGPMAVAFEVYDDFLHYKKGIYHHTGLRDPFNPFELTNHAVLLVGYGTDSASGMDYWIVKNSWGTGWGENGYFRIRRGTDECAIESIAVAATPIPKL","proteinLength":"Full Length","predictedMolecularWeight":"51 kDa","actualMolecularWeight":null,"aminoAcidEnd":463,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"P53634","tags":[{"tag":"His","terminus":"C-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Ambient - Can Ship with Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°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

Lyophilized

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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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Product promise

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