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HPN / TMPRSS1 / Hepsin Antibody
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P |
|---|---|
| Primary Accession | P05981 |
| Reactivity | Human, Rabbit, Monkey, Bovine, Dog |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 45kDa |
| Dilution | IHC-P (5 µg/ml), WB (1 µg/ml), |
| Gene ID | 3249 |
|---|---|
| Other Names | Serine protease hepsin, 3.4.21.106, Transmembrane protease serine 1, Serine protease hepsin non-catalytic chain, Serine protease hepsin catalytic chain, HPN, TMPRSS1 |
| Reconstitution & Storage | Short term 4°C, long term aliquot and store at -20°C, avoid freeze thaw cycles. |
| Precautions | HPN / TMPRSS1 / Hepsin Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | HPN |
|---|---|
| Synonyms | TMPRSS1 |
| Function | Serine protease that cleaves extracellular substrates, and contributes to the proteolytic processing of growth factors, such as HGF and MST1/HGFL (PubMed:15839837, PubMed:21875933). Plays a role in cell growth and maintenance of cell morphology (PubMed:21875933, PubMed:8346233). Plays a role in the proteolytic processing of ACE2 (PubMed:24227843). Mediates the proteolytic cleavage of urinary UMOD that is required for UMOD polymerization (PubMed:26673890). |
| Cellular Location | Cell membrane; Single-pass type II membrane protein Apical cell membrane; Single-pass type II membrane protein |
| Tissue Location | Detected in liver and kidney. |
| Volume | 100 µl |
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
Plays an essential role in cell growth and maintenance of cell morphology. May mediate the activating cleavage of HGF and MST1/HGFL. Plays a role in the proteolytic processing of ACE2.
References
Leytus S.P.,et al.Biochemistry 27:1067-1074(1988).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Tsuji A.,et al.J. Biol. Chem. 266:16948-16953(1991).
Torres-Rosado A.,et al.Proc. Natl. Acad. Sci. U.S.A. 90:7181-7185(1993).
Chen R.,et al.J. Proteome Res. 8:651-661(2009).
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