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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...

Affinity and Avidity

Affinity and Avidity

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...

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...

Hybridoma Technology

Hybridoma Technology

Hybridoma technology is used for the large-scale production of monoclonal antibodies. Monoclonal antibodies bind to only a single antigenic determinant or epitope. Such antibodies are used in research, diagnostics, and disease therapy. The hybridoma technology established in 1975 by Georges Köhler and Cesar Milstein was awarded the Nobel Prize in Medicine in 1984 for revolutionizing research and therapy.
Hybridoma Selection
Commonly used fusion techniques — electroporation, polyethylene glycol...

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Related Experiment Video

Updated: Jul 4, 2026

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

When binding is enough: nonactivating antibody formats.

Aran F Labrijn¹, Rob C Aalberse, Janine Schuurman

¹Genmab, Yalelaan 60, Utrecht, The Netherlands. a.labrijn@genmab.com

Current Opinion in Immunology

|June 26, 2008

Summary

This summary is machine-generated.

Therapeutic antibodies can be engineered as nonactivating, monovalent, or bivalent formats. This approach minimizes unwanted immune responses and potential target binding issues, improving therapeutic outcomes.

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Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study

Published on: June 29, 2016

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Last Updated: Jul 4, 2026

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Published on: January 14, 2020

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Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study

Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study

Published on: June 29, 2016

Area of Science:

Immunology
Biotechnology
Pharmacology

Background:

Most clinical therapeutic antibodies utilize the human IgG1 format, a bivalent molecule.
IgG1 antibodies engage immune effector functions, which is not always desirable for therapeutic efficacy.
Bivalent binding can sometimes hinder antibody therapeutic effectiveness.

Purpose of the Study:

To review nonactivating antibody therapeutics.
To discuss antibody formats that avoid immune system engagement.
To explore both monovalent and bivalent nonactivating antibody designs.

Main Methods:

Review of current literature on antibody engineering.
Analysis of antibody formats and their immune interactions.
Discussion of therapeutic applications for nonactivating antibodies.

Main Results:

Nonactivating antibody formats can be designed in monovalent or bivalent structures.
These engineered antibodies reduce unwanted immune system engagement.
Target binding can be modulated by format selection.

Conclusions:

Nonactivating antibody therapeutics offer an alternative to traditional IgG1 formats.
Monovalent and bivalent nonactivating designs provide flexibility for different therapeutic needs.
Engineering antibodies for reduced immune activation is a key strategy for improved therapies.