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Related Concept Videos

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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An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions
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New ELISA approach based on coiled-coil interactions.

Benoît Liberelle1, Laurence Bartholin, Cyril Boucher

  • 1Department of Chemical Engineering, Bio-P2 Research Unit, Institute of Biomedical Engineering, Groupe de Recherche en Sciences et Technologies Biomédicales, Ecole Polytechnique de Montréal, PO BOX 6079, Station Centre-ville, Montréal (QC) Canada H3C 3A7.

Journal of Immunological Methods
|September 28, 2010
PubMed
Summary

A novel Enzyme-Linked Immunosorbent Assay (ELISA) uses engineered E/K coiled-coil protein interactions for quantifying epidermal growth factor (EGF). This system offers improved plate reusability and storability compared to traditional methods.

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Area of Science:

  • Biochemistry
  • Protein Engineering
  • Assay Development

Background:

  • The E/K coiled-coil system is a versatile tool for protein capture and dimerization in biotech and pharma.
  • Existing methods for protein quantitation, like ELISA, often rely on antibodies or poly-histidine tags.

Purpose of the Study:

  • To develop a new generation of ELISA for direct quantitation of coil-tagged epidermal growth factor (EGF).
  • To evaluate the performance, specificity, and practical advantages of this coiled-coil based ELISA system.

Main Methods:

  • Development of an ELISA utilizing E/K coiled-coil interactions for direct protein quantitation.
  • Evaluation of specificity, plate storability, reusability, and convenience.
  • Comparison with standard antibody-based ELISA and Ni-NTA capture systems.
  • Validation of the E/K coiled-coil ELISA for recovery and assay variations.

Main Results:

  • The E/K coiled-coil ELISA demonstrated comparable affinity/sensitivity to antibody-based systems.
  • It showed improved affinity/sensitivity over the Ni-NTA capture system.
  • The system exhibited excellent plate storability and reusability.
  • A practical working range of 5.2–34,000 pM was established.

Conclusions:

  • The E/K coiled-coil ELISA system provides a robust and efficient method for quantitating coil-tagged proteins.
  • It presents a viable alternative to traditional tags like poly-histidine in ELISA development.
  • Enhanced plate stability and reusability make it a practical choice for various applications.