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Related Concept Videos

Antibody Structure01:10

Antibody Structure

61.7K
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...
61.7K
Antibody Structure and Classes01:25

Antibody Structure and Classes

5.7K
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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Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

3.5K
Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
3.5K
Transcytosis of IgG01:15

Transcytosis of IgG

3.0K
Transcytosis is the process in which molecules are internalized by endocytosis, transported across the cell, and released through exocytosis from the opposite end of the cell. Molecules such as insulin, immunoglobulins, and certain nutrients are transferred through the recycling endosomes by recycling and transcytosis.
IgG molecules from a mother undergo transcytosis starting around 13 weeks of gestation. The amount of IgG transferred and entering the fetal blood circulation increases with...
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Integrins01:10

Integrins

4.3K
Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
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Immunocytochemistry and Immunohistochemistry01:22

Immunocytochemistry and Immunohistochemistry

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Immunocytochemistry (ICC) and immunohistochemistry (IHC) are techniques that use antibodies to check for specific proteins or antigens in a sample. The technique was first published by Albert Coons in 1941 to detect the presence of pneumococcal antigen in tissue sections from mice infected with Pneumococcus. Immunocytochemistry helps localization of proteins or antigens in individual cells like blood cells, stem cells, etc., while immunohistochemistry does the same for tissue samples.
These...
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Related Experiment Video

Updated: Oct 10, 2025

Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy
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Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy

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3D Structures of IgA, IgM, and Components.

Shunli Pan1, Noriyoshi Manabe1, Yoshiki Yamaguchi1

  • 1Division of Structural Glycobiology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Medical and Pharmaceutical University, 4-4-1 Komatsushima, Aoba-ku, Sendai 981-8558, Miyagi, Japan.

International Journal of Molecular Sciences
|December 10, 2021
PubMed
Summary
This summary is machine-generated.

Immunoglobulin A (IgA) and Immunoglobulin M (IgM) are crucial for mucosal immunity. Advances in structural biology are revealing their complex 3D structures, paving the way for new antibody therapeutics.

Keywords:
3D structureIgAIgMJ-chaindisulfide bridgeglycosylationmolecular assemblysecretory component

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Immunoglobulin G N-Glycan Analysis by Ultra-Performance Liquid Chromatography
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Area of Science:

  • Structural Biology
  • Immunology
  • Biochemistry

Background:

  • Immunoglobulin G (IgG) is widely used in therapeutics, but Immunoglobulin A (IgA) and Immunoglobulin M (IgM) play key roles in mucosal immunity.
  • IgA and IgM possess complex structures, often assembled as dimers or pentamers with joining (J)-chains and secretory components (SC).
  • Previous 3D structural studies of IgA and IgM at atomic resolution have been limited due to their complexity.

Purpose of the Study:

  • To examine the 3D structures of IgA and IgM, including their associated J-chains and SC.
  • To summarize disulfide bridging and N-glycosylation patterns in IgA and IgM.
  • To highlight the accumulating structural information and its implications for therapeutic applications.

Main Methods:

  • Review and examination of existing 3D structural data for IgA and IgM.
  • Analysis of structural components such as J-chains and secretory components (SC).
  • Summarization of post-translational modifications including disulfide bonds and N-glycosylation.

Main Results:

  • Detailed examination of the 3D structures of IgA-Fc and IgM-Fc regions.
  • Compilation of information on the roles of J-chains and SC in IgA and IgM assembly and transport.
  • Summary of critical disulfide bridging and N-glycosylation sites influencing structure and function.

Conclusions:

  • Atomic-scale structural insights into IgA and IgM are rapidly increasing.
  • Understanding the structure-function relationships of IgA and IgM is crucial for their therapeutic potential.
  • IgA- and IgM-based monoclonal antibodies represent a promising future direction for therapeutic development.