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Related Concept Videos

Antibody Actions01:26

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...
Antibody Structure01:10

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 Technology01:31

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...
Antibody Structure and Classes01:25

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.
Affinity and Avidity01:41

Affinity and Avidity

Overview
Immunoprecipitation01:20

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...

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Related Experiment Video

Updated: May 9, 2026

Generation of Discriminative Human Monoclonal Antibodies from Rare Antigen-specific B Cells Circulating in Blood
13:14

Generation of Discriminative Human Monoclonal Antibodies from Rare Antigen-specific B Cells Circulating in Blood

Published on: February 6, 2018

Toward aggregation-resistant antibodies by design.

Christine C Lee1, Joseph M Perchiacca, Peter M Tessier

  • 1Center for Biotechnology & Interdisciplinary Studies, Department of Chemical & Biological Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.

Trends in Biotechnology
|August 13, 2013
PubMed
Summary
This summary is machine-generated.

Engineered monoclonal antibodies show improved solubility and reduced aggregation, enhancing their therapeutic potential. Rational design strategies are key to developing more stable and effective antibody-based medicines.

Keywords:
FabFvIgGV(H)V(L)antibody engineeringbispecificcomplementarity-determining region (CDR)monoclonal antibodyscFvsolubilityvariable domain

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Targeted Antibody Blocking by a Dual-Functional Conjugate of Antigenic Peptide and Fc-III Mimetics (DCAF)

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Single-cell Screening Method for the Selection and Recovery of Antibodies with Desired Specificities from Enriched Human Memory B Cell Populations
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Single-cell Screening Method for the Selection and Recovery of Antibodies with Desired Specificities from Enriched Human Memory B Cell Populations

Published on: August 22, 2019

Related Experiment Videos

Last Updated: May 9, 2026

Generation of Discriminative Human Monoclonal Antibodies from Rare Antigen-specific B Cells Circulating in Blood
13:14

Generation of Discriminative Human Monoclonal Antibodies from Rare Antigen-specific B Cells Circulating in Blood

Published on: February 6, 2018

Targeted Antibody Blocking by a Dual-Functional Conjugate of Antigenic Peptide and Fc-III Mimetics (DCAF)
09:39

Targeted Antibody Blocking by a Dual-Functional Conjugate of Antigenic Peptide and Fc-III Mimetics (DCAF)

Published on: September 17, 2019

Single-cell Screening Method for the Selection and Recovery of Antibodies with Desired Specificities from Enriched Human Memory B Cell Populations
09:07

Single-cell Screening Method for the Selection and Recovery of Antibodies with Desired Specificities from Enriched Human Memory B Cell Populations

Published on: August 22, 2019

Area of Science:

  • Biotechnology
  • Protein Engineering
  • Immunology

Background:

  • Monoclonal antibodies (mAbs) are potent therapeutics with high specificity and affinity.
  • Antibody aggregation during purification and delivery is a significant challenge, limiting their clinical application.
  • Current methods for improving antibody solubility are often empirical and unpredictable.

Purpose of the Study:

  • To review advances in engineering antibody fragments and full-length antibodies to resist aggregation.
  • To identify challenges and opportunities in developing aggregation-resistant antibody therapeutics.
  • To explore the role of rational design in enhancing antibody solubility without compromising binding affinity.

Main Methods:

  • Review of experimental and computational studies on antibody engineering for solubility.
  • Analysis of strategies targeting variable and constant antibody regions.
  • Examination of structure-function relationships in antibody aggregation.

Main Results:

  • Rational design methods can significantly improve antibody solubility and reduce aggregation.
  • Engineering efforts can enhance stability without sacrificing binding affinity.
  • Key advances have been made in understanding and mitigating antibody aggregation.

Conclusions:

  • Developing aggregation-resistant antibodies is crucial for advancing antibody-based therapies.
  • Integrated experimental and computational approaches are vital for rational antibody design.
  • Further development of predictive algorithms will accelerate the creation of robust antibody therapeutics.