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Antibody Actions

Antibody Actions

Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...

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.

Antibody Structure and Classes

Antibody Structure and Classes

Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.

Antibody Structure

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...

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 and Avidity

Affinity and Avidity

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Related Experiment Video

Updated: Jun 3, 2026

Genetic Encoding of a Non-Canonical Amino Acid for the Generation of Antibody-Drug Conjugates Through a Fast Bioorthogonal Reaction

Genetic Encoding of a Non-Canonical Amino Acid for the Generation of Antibody-Drug Conjugates Through a Fast Bioorthogonal Reaction

Published on: September 14, 2018

Antibody-enzyme conjugate formation.

¹Department of Biochemistry, The Queen's University of Belfast, Medical Biology Centre, Belfast, Ireland, UK.

Methods in Molecular Biology (Clifton, N.J.)

|March 15, 2011

Summary

Creating ideal antibody-enzyme conjugates is challenging. This study reviews and modifies three common labeling methods to improve immunoreactivity, enzyme activity, and stability for better diagnostic tools.

Area of Science:

Bioconjugation Chemistry
Immunodiagnostics

Background:

Antibody-enzyme conjugates are crucial for immunoassays.
Existing labeling methods often compromise antibody or enzyme function.
Achieving optimal conjugate properties (activity, stability, stoichiometry) remains a challenge.

Purpose of the Study:

To present modified, commonly used methods for antibody-enzyme conjugation.
To optimize labeling procedures for improved conjugate characteristics.

Main Methods:

Review and modification of three established immunoglobulin G (IgG) enzyme labeling techniques.
Exploitation of functional groups (amino, thiol, saccharide) on proteins.
Utilization of bifunctional reagents for enzyme-IgG linkage.

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Chemical Conjugation of a Purified DEC-205-Directed Antibody with Full-Length Protein for Targeting Mouse Dendritic Cells In Vitro and In Vivo

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Genetic Encoding of a Non-Canonical Amino Acid for the Generation of Antibody-Drug Conjugates Through a Fast Bioorthogonal Reaction

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Main Results:

The presented modifications aim to enhance retention of immunoreactivity and enzyme activity.
The goal is to achieve defined and appropriate proportions in the conjugates.
Improved stability of the antibody-enzyme conjugates is anticipated.

Conclusions:

Modified labeling methods offer a pathway to superior antibody-enzyme conjugates.
These optimized conjugates are expected to improve the performance of diagnostic assays.
Further refinement of conjugation techniques is essential for advancing immunodiagnostics.