TMPRSS9 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
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Primary Accession | Q7Z410 |
Other Accession | NP_892018.1 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 114021 Da |
Antigen Region | 124-153 aa |
Gene ID | 360200 |
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Other Names | Transmembrane protease serine 9, 3421-, Polyserase-I, Polyserine protease 1, Polyserase-1, Serase-1, Serase-2, Serase-3, TMPRSS9 |
Target/Specificity | This TMPRSS9 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 124-153 amino acids from the N-terminal region of human TMPRSS9. |
Dilution | WB~~1:1000 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | TMPRSS9 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | TMPRSS9 |
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Function | Serase-1 and serase-2 are serine proteases that hydrolyze the peptides N-t-Boc-Gln-Ala-Arg-AMC and N-t-Boc-Gln-Gly-Arg-AMC. In contrast, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Ala-Pro-Ala-AMC are not significantly hydrolyzed. |
Cellular Location | Cell membrane; Single-pass type II membrane protein |
Tissue Location | Expressed in fetal human tissues, such as kidney, liver, lung and brain, and in a variety of tumor cell lines. Weakly expressed in adult tissues including skeletal muscle, liver, placenta and heart. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Serase-1 and serase-2 are serine proteases that hydrolyze the peptides N-t-Boc-Gln-Ala-Arg-AMC and N-t-Boc-Gln-Gly-Arg-AMC. In contrast, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Ala-Pro-Ala-AMC are not significantly hydrolyzed.
References
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :
Okumura, Y., et al. Biochem. J. 400(3):551-561(2006)
Cal, S., et al. Proc. Natl. Acad. Sci. U.S.A. 100(16):9185-9190(2003)
Cal, S., et al. Proc. Natl. Acad. Sci. U.S.A. 100(16):9185-9190(2003)
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