Enterokinase Inhibitor Assay Kit (Fluorometric) (ab170965)

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Inhibition of Enteropeptidase

    Key features and details

    • Assay type: Enzyme activity
    • Detection method: Fluorescent
    • Platform: Microplate reader
    • Sample type: Inhibitor compounds

    Overview

    • Product name

      Enterokinase Inhibitor Assay Kit (Fluorometric)
      See all Enterokinase kits

    • Detection method

      Fluorescent

    • Sample type

      Inhibitor compounds

    • Assay type

      Enzyme activity

    • Product overview

      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.

    • Notes

      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.

    • Platform

      Microplate reader

    Properties

    • Storage instructions

      Store 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

    • Research areas

    • 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.

    • Tissue specificity

      Intestinal brush border.

    • Involvement in disease

      Defects 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 similarities

      Belongs 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.

    • Post-translational
      modifications

      The chains are derived from a single precursor that is cleaved by a trypsin-like protease.

    • Cellular localization

      Membrane.
    • Information by UniProt

    • Alternative names

      • PRSS 7
      • PRSS7
      • Enterokinase
      • Enterokinase catalytic subunit
      • Enteropeptidase
      • Enteropeptidase catalytic light chain
      • Enteropeptidase non catalytic heavy chain
      • ENTK
      • ENTK_HUMAN
      • PROENTEROKINASE
      • protease, serine, 7 (enterokinase)
      • PRSS7
      • Serine protease 7
      • TMPRSS15
      • Transmembrane protease serine 15
      see all

    Images

    • Inhibition of Enteropeptidase
      Inhibition of Enteropeptidase

      Inhibition of Enteropeptidase activity by Enteropeptidase-specific Inhibitor, Aprotinin. Assay was performed following kit protocol.

    References (0)

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    ab170965 has not yet been referenced specifically in any publications.

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