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Related Concept Videos

Antibody Structure and Classes01:25

Antibody Structure and Classes

6.1K
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.
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Antibody Structure01:10

Antibody Structure

61.8K
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...
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Diversity of Antigen Receptors01:28

Diversity of Antigen Receptors

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Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
938
Affinity and Avidity01:41

Affinity and Avidity

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Overview
37.0K
Antibody Actions01:26

Antibody Actions

1.6K
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...
1.6K
Hybridoma Technology01:31

Hybridoma Technology

15.8K
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,...
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Related Experiment Video

Updated: Oct 15, 2025

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
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Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing

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Micro-Heterogeneity of Antibody Molecules.

Yusuke Mimura1, Radka Saldova2,3, Yuka Mimura-Kimura4

  • 1Department of Clinical Research, National Hospital Organization Yamaguchi Ube Medical Center, Ube, Japan. mimura.yusuke.qy@mail.hosp.go.jp.

Experientia Supplementum (2012)
|October 23, 2021
PubMed
Summary

Therapeutic monoclonal antibodies (mAbs) require comprehensive characterization of post-translational modifications (PTMs) to ensure consistent efficacy and safety. Understanding PTMs is crucial for maintaining critical quality attributes throughout a drug

Keywords:
Critical quality attributesGlycoformsGlycoproteinsOligosaccharidesPosttranslational modificationsRecombinant antibody therapeutics

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Area of Science:

  • Biopharmaceutical development
  • Protein chemistry
  • Immunology

Background:

  • Therapeutic monoclonal antibodies (mAbs) are vital IgG biopharmaceuticals.
  • mAbs undergo post-translational modifications (PTMs) leading to heterogeneity.
  • Recombinant mAb production can alter structural fidelity and biological activity.

Purpose of the Study:

  • To review common PTMs in mAbs and endogenous IgG.
  • To explore the relationship between mAb structural variants and clinical performance.
  • To emphasize the importance of PTM characterization for regulatory approval and drug product consistency.

Main Methods:

  • Review of current literature on mAb PTMs.
  • Analysis of orthogonal analytical technologies for mAb characterization.
  • Discussion of quality by design principles for PTM control.

Main Results:

  • PTMs, especially glycosylation at Asn297, are critical quality attributes (CQAs) impacting mAb efficacy and safety.
  • Mammalian cell-produced mAbs exhibit less heterogeneity than serum-derived IgG.
  • Maintaining a consistent PTM profile is essential for drug product lifespan.

Conclusions:

  • Comprehensive structural characterization of mAbs, including PTMs, is mandated by regulatory authorities.
  • Control of PTMs is key to ensuring the stability, activity, and immunogenicity profile of therapeutic mAbs.
  • Understanding PTM-clinical performance relationships is vital for successful biopharmaceutical development.