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Enzyme-Linked Immunosorbent Assay01:33

Enzyme-Linked Immunosorbent Assay

In 1971, Peter Perlman and Eva Engvall developed an Enzyme-linked immunosorbent assay (ELISA or EIA). ELISA differs from western blot in that the assays are conducted in microtiter plates or in vivo rather than on an absorbent membrane.
There are many different types of ELISAs, but they all involve an antibody molecule whose constant region binds an enzyme, leaving the variable region free to bind its specific antigen.  Enzyme-substrate reaction allows the antigen to be visualized or quantified.

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Related Experiment Video

Updated: May 14, 2026

Quantifying the Modulation of Elastase Enzyme Activity Through Colorimetric Analysis
04:30

Quantifying the Modulation of Elastase Enzyme Activity Through Colorimetric Analysis

Published on: January 17, 2025

A methodology for detection and quantification of esterase activity.

Ana L Simplício1, Ana S Coroadinha, John F Gilmer

  • 1Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal. anas@itqb.unl.pt

Methods in Molecular Biology (Clifton, N.J.)
|February 7, 2013
PubMed
Summary

Quantifying carboxylesterase 2 activity is crucial for cancer research, as enzyme levels don't always reflect function. This study introduces a method to specifically measure carboxylesterase 2 activity, even among other esterases.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Pharmacology

Background:

  • Carboxylesterases (CES) are vital enzymes in xenobiotic metabolism.
  • CES activity is increasingly relevant for cancer therapies.
  • Accurate quantification of individual CES activity is essential due to variations and poor correlation with protein levels.

Purpose of the Study:

  • To develop and present a methodology for specifically quantifying carboxylesterase 2 (CES2) activity.
  • To demonstrate the method's applicability in assessing interspecies variations and transfected cell extracts.

Main Methods:

  • Development of a specific assay for carboxylesterase 2 activity.
  • Utilizing selective substrates and/or inhibitors for esterase differentiation.
  • Application of the methodology to evaluate interspecies differences and enzyme activity in cell extracts.

Main Results:

  • A robust methodology for the specific quantification of carboxylesterase 2 activity was established.
  • The method successfully differentiated CES2 activity within a mixture of esterases.
  • Applicability demonstrated for interspecies variation analysis and transfected cell enzyme activity assessment.

Conclusions:

  • The presented methodology enables precise measurement of carboxylesterase 2 activity.
  • This tool is valuable for research in xenobiotic metabolism and cancer therapy development.
  • The approach is adaptable for quantifying other esterase activities with appropriate substrate/inhibitor selection.