Enterokinase/Enteropeptidase Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
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Application ![]()
| WB, E |
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Primary Accession | P98073 |
Other Accession | NP_002763 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 112935 Da |
Antigen Region | 972-1002 aa |
Gene ID | 5651 |
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Other Names | Enteropeptidase, Enterokinase, Serine protease 7, Transmembrane protease serine 15, Enteropeptidase non-catalytic heavy chain, Enteropeptidase catalytic light chain, TMPRSS15, ENTK, PRSS7 |
Target/Specificity | This Enterokinase/Enteropeptidase antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 972~1002 amino acids from the C-terminal region of human enteropeptidase. |
Dilution | WB~~1:1000 E~~Use at an assay dependent concentration. |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
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 | Enterokinase/Enteropeptidase Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | TMPRSS15 |
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Synonyms | ENTK, PRSS7 |
Function | Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases. |
Cellular Location | Membrane; Single-pass type II membrane protein |
Tissue Location | Intestinal brush border. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
This enzyme converts the pancreatic proenzyme trypsinogen to trypsin, which activates other proenzymes including chymotrypsinogen and procarboxypeptidases. The precursor protein is cleaved into two chains that form a heterodimer linked by a disulfide bond. This protein is a member of the trypsin family of peptidases. Mutations in this gene cause enterokinase deficiency, a malabsorption disorder characterized by diarrhea and failure to thrive.
REFERENCES
Holzinger, A., et al., Am. J. Hum. Genet. 70(1):20-25 (2002).
Kitamoto, Y., et al., Biochemistry 34(14):4562-4568 (1995).
Kitamoto, Y., et al., Proc. Natl. Acad. Sci. U.S.A. 91(16):7588-7592 (1994).
Imamura, T., et al., Am. J. Physiol. Gastrointest. Liver Physiol. 285 (6), G1235-G1241 (2003) (): ().
Freeman, T.C., et al., Clin. Chim. Acta 195 (1-2), 27-39 (1990) (): ().

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