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Related Concept Videos

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 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
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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...
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...
Cross-reactivity00:42

Cross-reactivity

Overview
Humoral Immune Responses01:36

Humoral Immune Responses

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Related Experiment Video

Updated: May 15, 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

Antibody Humanization.

Tim D Jones1

  • 1Babraham, Cambridge, UK. drtdjones@gmail.com.

Methods in Molecular Biology (Clifton, N.J.)
|May 13, 2026
PubMed
Summary
This summary is machine-generated.

Antibody humanization engineers animal antibodies to resemble human ones, reducing immune responses in patients. This process refines antibody structure and binding for clinical use.

Keywords:
ADAAcceptorAntibodyCDRDonorFrameworkGraftingHumanisation

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Last Updated: May 15, 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

Laboratory Scale Production and Purification of a Therapeutic Antibody
09:54

Laboratory Scale Production and Purification of a Therapeutic Antibody

Published on: January 24, 2017

Generation of Recombinant Human IgG Monoclonal Antibodies from Immortalized Sorted B Cells
10:32

Generation of Recombinant Human IgG Monoclonal Antibodies from Immortalized Sorted B Cells

Published on: June 5, 2015

Area of Science:

  • Biotechnology
  • Immunology
  • Protein Engineering

Background:

  • Antibodies from animal species, typically murine, can trigger adverse immune reactions when administered to humans.
  • Developing therapeutic antibodies requires minimizing immunogenicity to ensure patient safety and treatment efficacy.

Purpose of the Study:

  • To describe the process of antibody humanization for therapeutic applications.
  • To explain methods for engineering animal antibodies to reduce immunogenicity in humans.

Main Methods:

  • Selecting appropriate human antibody sequences as acceptor templates.
  • Identifying critical murine amino acids, including CDRs and framework residues, for retention to preserve antigen binding.
  • Optimizing physicochemical properties of the antibody during the humanization process.

Main Results:

  • Engineered antibodies exhibit reduced immunogenicity compared to original animal antibodies.
  • Preservation of antigen-binding affinity is achieved through strategic amino acid selection.
  • Improved antibody characteristics enhance suitability for clinical applications.

Conclusions:

  • Antibody humanization is a crucial technique for developing safe and effective antibody-based therapeutics.
  • The described methods allow for the successful modification of animal antibodies into human-like structures.
  • Careful consideration of structural and physicochemical factors is essential for successful antibody humanization.