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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.

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Related Experiment Video

Updated: Jun 4, 2026

SDS-PAGE/Immunoblot Detection of Aβ Multimers in Human Cortical Tissue Homogenates using Antigen-Epitope Retrieval

SDS-PAGE/Immunoblot Detection of Aβ Multimers in Human Cortical Tissue Homogenates using Antigen-Epitope Retrieval

Published on: April 23, 2010

Quantifying Aβ(1-40) and Aβ (1-42) Using Sandwich-ELISA.

D M Skovronsky¹, J Wang, V M Lee

¹Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, PA.

Methods in Molecular Medicine

|February 15, 2011

Summary

This summary is machine-generated.

Alzheimer's disease pathogenesis involves amyloid-beta (Aβ) accumulation. This study introduces a sensitive sandwich-ELISA to differentiate and quantify Aβ(1-40) and Aβ(1-42) in various biological samples.

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Last Updated: Jun 4, 2026

SDS-PAGE/Immunoblot Detection of Aβ Multimers in Human Cortical Tissue Homogenates using Antigen-Epitope Retrieval

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Absolute Quantification of Aβ1-42 in CSF Using a Mass Spectrometric Reference Measurement Procedure

Absolute Quantification of Aβ_1-42 in CSF Using a Mass Spectrometric Reference Measurement Procedure

Published on: March 21, 2017

Area of Science:

Neuroscience
Biochemistry
Genetics

Background:

Amyloid-beta (Aβ) accumulation is implicated in Alzheimer's disease (AD) pathogenesis.
Familial AD (FAD) mutations in APP, PS1, and PS2 genes alter Aβ production, favoring Aβ(1-42) over Aβ(1-40).
Differential deposition of Aβ(1-40) and Aβ(1-42) in senile plaques suggests their crucial role in AD.

Purpose of the Study:

To develop and validate a sensitive method for quantifying specific Aβ peptide species.
To differentiate between the production and deposition of Aβ(1-40) and Aβ(1-42).

Main Methods:

Development of a highly sensitive sandwich-enzyme-linked immunosorbent assay (ELISA).
Quantification of Aβ(1-40) and Aβ(1-42) in soluble and insoluble pools.
Analysis of Aβ peptides in cultured cell media, cerebrospinal fluid (CSF), intracellular pools, and brain parenchyma.

Main Results:

The developed sandwich-ELISA accurately quantifies both Aβ(1-40) and Aβ(1-42).
The assay is applicable to diverse biological matrices, including cell culture media, CSF, and brain tissue.
Enables precise measurement of differential Aβ peptide production and deposition.

Conclusions:

A sensitive sandwich-ELISA is crucial for studying AD pathogenesis by differentiating Aβ(1-40) and Aβ(1-42).
This method facilitates research into the specific roles of different Aβ isoforms in AD.
Accurate quantification of Aβ peptides is essential for understanding disease mechanisms and developing therapeutic strategies.