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Enzyme-Linked Immunosorbent Assay

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.

Immunoprecipitation

Immunoprecipitation

Immunoprecipitation, or IP, is a widely used technique that employs protein-antibody interactions to isolate proteins or protein complexes in their native state for studying protein-protein interactions, quaternary structures, or supramolecular complexes. Various modifications of the technique, including chromatin IP, cross-linking IP, and fluorescence IP, are commonly used.
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...

Affinity Chromatography

Affinity Chromatography

Affinity chromatography is a powerful technique extensively utilized for separating and purifying specific biomolecules from complex mixtures. It capitalizes on the highly selective binding between an analyte and its counterpart, such as antibody-antigen interactions. The counterpart is immobilized on the stationary phase, forming an affinity column. The stationary phase typically consists of solid support, such as agarose or porous glass beads, immobilizing the affinity ligand. The mobile...

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Related Experiment Video

Updated: Jun 7, 2026

Characterization of Thymus-dependent and Thymus-independent Immunoglobulin Isotype Responses in Mice Using Enzyme-linked Immunosorbent Assay

Characterization of Thymus-dependent and Thymus-independent Immunoglobulin Isotype Responses in Mice Using Enzyme-linked Immunosorbent Assay

Published on: September 7, 2018

Immunoassays using polypeptide conjugate binders with tuned affinity.

Ken Cham Fai Leung¹, Ho Pui Ho, Yiu Wa Kwan

¹Center of Novel Functional Molecules, The Chinese University of Hong Kong, Shatin, NT, Hong Kong.

Expert Review of Molecular Diagnostics

|October 23, 2010

Summary

This summary is machine-generated.

Researchers developed a novel polypeptide conjugate binder for high-affinity protein detection in immunoassays. This innovative assay design offers tunable affinity for improved clinical diagnostics and disease marker detection.

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Last Updated: Jun 7, 2026

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Area of Science:

Biotechnology and Biomedical Engineering
Molecular Biology and Biochemistry
Analytical Chemistry

Background:

Immunoassays are crucial for detecting disease biomarkers.
Existing methods like ELISA have limitations in sensitivity and specificity.
Novel recognition elements are needed for advanced clinical diagnostics.

Discussion:

This study introduces polypeptide conjugates as high-affinity binders for immunoassays.
These hybrid molecules combine a recognition ligand with a synthetic polypeptide for target binding.
The binding affinity can be modulated by altering the spacer length between the ligand and polypeptide.

Key Insights:

Polypeptide conjugates offer tunable, high-affinity, and selective protein recognition.
This approach presents an alternative to traditional antibody-based detection methods.
Comparison with ELISA, bio-barcode, and aptamer assays highlights the pros and cons of this new technique.

Outlook:

Further innovation in materials and technologies is expected for novel disease marker detection.
Integration of polypeptide conjugates could lead to more sensitive and specific diagnostic tools.
This approach holds promise for advancing clinical diagnostics and personalized medicine.