| Description |
Enteropeptidase (Enterokinase, EC 3.4.21.9) is a serine protease involved in activation of trypsinogen to trypsin, which in turn results in the activation of various digestive enzymes. It recognizes a highly specific amino acid sequence ‘DDDDK’ and cleaves after the lysine residue. High specific activity of Enteropeptidase has been utilized in cleaving a variety of native or fusion proteins containing the above recognition. In Biovision’s Enteropeptidase inhibitor screening kit, we have utilized a peptide substrate containing the Enteropeptidase recognition sequence along with a fluorescent label ‘AFC’. Enteropeptidase catalyzes the cleavage of this substrate and releases the AFC molecule, which can be easily quantified by measuring its fluorescence at Ex/Em = 380/500 nm. In the presence of potent Enteropeptidase inhibitor, the hydrolyzation of the substrate will be impeded. The kit provides a rapid, simple & reliable test for screening potential inhibitors of Enteropeptidase.
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