|Other Names||Enteropeptidase, Enterokinase, Serine protease 7, Transmembrane protease serine 15, Enteropeptidase non-catalytic heavy chain, Enteropeptidase catalytic light chain, TMPRSS15, ENTK, PRSS7|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|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.|
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Provided below are standard protocols that you may find useful for product applications.
This gene encodes an enzyme that converts the pancreaticproenzyme trypsinogen to trypsin, which activates other proenzymesincluding chymotrypsinogen and procarboxypeptidases. The precursorprotein is cleaved into two chains that form a heterodimer linkedby a disulfide bond. This protein is a member of the trypsin familyof peptidases. Mutations in this gene cause enterokinasedeficiency, a malabsorption disorder characterized by diarrhea andfailure to thrive.
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :Nakanishi, J., et al. J. Invest. Dermatol. 130(4):944-952(2010)Vilen, S.T., et al. Exp. Cell Res. 314(4):914-926(2008)Imamura, T., et al. Am. J. Physiol. Gastrointest. Liver Physiol. 285 (6), G1235-G1241 (2003) :Holzinger, A., et al. Am. J. Hum. Genet. 70(1):20-25(2002)
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