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CTSC / Cathepsin C / JP Antibody (aa238-252)
Goat Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| IHC-P, E |
|---|---|
| Primary Accession | P53634 |
| Reactivity | Human, Monkey |
| Host | Goat |
| Clonality | Polyclonal |
| Calculated MW | 52kDa |
| Dilution | ELISA (1:128000), IHC-P (5 µg/ml), |
| Gene ID | 1075 |
|---|---|
| Other Names | Dipeptidyl peptidase 1, 3.4.14.1, Cathepsin C, Cathepsin J, Dipeptidyl peptidase I, DPP-I, DPPI, Dipeptidyl transferase, Dipeptidyl peptidase 1 exclusion domain chain, Dipeptidyl peptidase I exclusion domain chain, Dipeptidyl peptidase 1 heavy chain, Dipeptidyl peptidase I heavy chain, Dipeptidyl peptidase 1 light chain, Dipeptidyl peptidase I light chain, CTSC, CPPI |
| Target/Specificity | Human CTSC / Cathepsin C / JP. This antibody is expected to recognize isoform a (NP_001805.3) only. |
| Reconstitution & Storage | Store at -20°C. Minimize freezing and thawing. |
| Precautions | CTSC / Cathepsin C / JP Antibody (aa238-252) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | CTSC |
|---|---|
| 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. |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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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.
References
Paris A.,et al.FEBS Lett. 369:326-330(1995).
Rao N.V.,et al.J. Biol. Chem. 272:10260-10265(1997).
Allende L.M.,et al.Hum. Mutat. 17:152-153(2001).
Allende L.M.,et al.Mol. Genet. Metab. 79:146-148(2003).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
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