Cleaved-Cathepsin C HC (R394) Polyclonal Antibody
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Application ![]()
| WB |
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Primary Accession | P53634 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 51854 Da |
Gene ID | 1075 |
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Other Names | CTSC; CPPI; Dipeptidyl peptidase 1; Cathepsin C; Cathepsin J; Dipeptidyl peptidase I; DPP-I; DPPI; Dipeptidyl transferase |
Dilution | WB~~Western Blot: 1/500 - 1/2000. ELISA: 1/20000. Not yet tested in other applications. |
Format | Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.09% (W/V) sodium azide. |
Storage Conditions | -20℃ |
Name | CTSC |
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Synonyms | CPPI |
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). |
Cellular Location | Lysosome. |
Tissue Location | Ubiquitous. Highly expressed in lung, kidney and placenta. Detected at intermediate levels in colon, small intestine, spleen and pancreas. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII.

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