Product nameEnterokinase Inhibitor Assay Kit (Fluorometric)
See all Enterokinase kits
Sample typeInhibitor compounds
Assay typeEnzyme activity
Abcam's Enterokinase Inhibitor Screening Kit (Fluorometric) utilizes 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 and reliable test for screening potential inhibitors of Enteropeptidase.
Enteropeptidase (Enterokinase, EC 126.96.36.199) 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.
Storage instructionsStore at -20°C. Please refer to protocols.
Components Identifier 100 tests Enteropeptidase Assay Buffer WM 1 x 20ml Enteropeptidase Substrate Red 1 x 0.2ml Enteropeptidase-specific Inhibitor [Aprotinin] Blue 1 x 0.1ml Human Enteropeptidase Green 1 x 0.17ml
FunctionResponsible 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.
Tissue specificityIntestinal brush border.
Involvement in diseaseDefects in TMPRSS15 are a cause of enterokinase deficiency (ENTKD) [MIM:226200]; a life-threatening intestinal malabsorption disorder characterized by diarrhea and failure to thrive.
Sequence similaritiesBelongs to the peptidase S1 family.
Contains 2 CUB domains.
Contains 2 LDL-receptor class A domains.
Contains 1 MAM domain.
Contains 1 peptidase S1 domain.
Contains 1 SEA domain.
Contains 1 SRCR domain.
modificationsThe chains are derived from a single precursor that is cleaved by a trypsin-like protease.
- Information by UniProt
- Enteropeptidase catalytic light chain
ab170965 has not yet been referenced specifically in any publications.