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TMPRSS11D / HAT Antibody (internal region)
Peptide-affinity purified goat antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| E |
|---|---|
| Primary Accession | O60235 |
| Other Accession | NP_004253.1, 9407 |
| Predicted | Human |
| Host | Goat |
| Clonality | Polyclonal |
| Concentration | 0.5 mg/ml |
| Isotype | IgG |
| Calculated MW | 46263 Da |
| Gene ID | 9407 |
|---|---|
| Other Names | Transmembrane protease serine 11D, 3.4.21.-, Airway trypsin-like protease, Transmembrane protease serine 11D non-catalytic chain, Transmembrane protease serine 11D catalytic chain, TMPRSS11D, HAT |
| Format | 0.5 mg/ml in Tris saline, 0.02% sodium azide, pH7.3 with 0.5% bovine serum albumin |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | TMPRSS11D / HAT Antibody (internal region) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | TMPRSS11D |
|---|---|
| Synonyms | HAT |
| Function | May play some biological role in the host defense system on the mucous membrane independently of or in cooperation with other substances in airway mucous or bronchial secretions. Plays a role in the proteolytic processing of ACE2. Proteolytically cleaves and activates the human coronavirus 229E (HCoV-229E) spike glycoprotein which facilitate virus-cell membrane fusions; spike proteins are synthesized and maintained in precursor intermediate folding states and proteolysis permits the refolding and energy release required to create stable virus-cell linkages and membrane coalescence. Preferentially cleaves the C-terminal side of arginine residues at the P1 position of certain peptides, cleaving Boc-Phe-Ser-Arg-4-methylcoumaryl-7-amide most efficiently and having an optimum pH of 8.6 with this substrate. |
| Cellular Location | Cell membrane; Single-pass type II membrane protein. Note=Activated by cleavage and secreted |
| Tissue Location | Located in the cells of the submucosal serous glands of the bronchi and trachea |
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.
References
Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium. Böttcher E, Matrosovich T, Beyerle M, Klenk HD, Garten W, Matrosovich M. J Virol. 2006 Oct;80(19):9896-8. PMID: 16973594
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