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Related Concept Videos

Enzyme-Linked Immunosorbent Assay01:33

Enzyme-Linked Immunosorbent Assay

In 1971, Peter Perlman and Eva Engvall developed an Enzyme-linked immunosorbent assay (ELISA or EIA). ELISA differs from western blot in that the assays are conducted in microtiter plates or in vivo rather than on an absorbent membrane.
There are many different types of ELISAs, but they all involve an antibody molecule whose constant region binds an enzyme, leaving the variable region free to bind its specific antigen.  Enzyme-substrate reaction allows the antigen to be visualized or quantified.
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

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...
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...
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...
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.

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Related Experiment Video

Updated: May 11, 2026

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
08:51

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

Published on: March 15, 2019

IgBLAST: an immunoglobulin variable domain sequence analysis tool.

Jian Ye1, Ning Ma, Thomas L Madden

  • 1National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA. jianye@ncbi.nlm.nih.gov

Nucleic Acids Research
|May 15, 2013
PubMed
Summary
This summary is machine-generated.

IgBLAST is a new tool for analyzing immunoglobulin (IG) sequences. It simplifies identifying V, D, and J genes and analyzing sequence variations, overcoming limitations of general tools like BLAST.

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VDJ-Seq: Deep Sequencing Analysis of Rearranged Immunoglobulin Heavy Chain Gene to Reveal Clonal Evolution Patterns of B Cell Lymphoma

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Last Updated: May 11, 2026

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
08:51

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

Published on: March 15, 2019

Immunoglobulin Gene Sequence Analysis In Chronic Lymphocytic Leukemia: From Patient Material To Sequence Interpretation
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Immunoglobulin Gene Sequence Analysis In Chronic Lymphocytic Leukemia: From Patient Material To Sequence Interpretation

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VDJ-Seq: Deep Sequencing Analysis of Rearranged Immunoglobulin Heavy Chain Gene to Reveal Clonal Evolution Patterns of B Cell Lymphoma
15:07

VDJ-Seq: Deep Sequencing Analysis of Rearranged Immunoglobulin Heavy Chain Gene to Reveal Clonal Evolution Patterns of B Cell Lymphoma

Published on: December 28, 2015

Area of Science:

  • Immunology
  • Bioinformatics
  • Genomics

Background:

  • Immunoglobulin (IG) sequence analysis involves identifying variable (V), diversity (D), and joining (J) genes.
  • Standard tools like BLAST are inefficient for IG sequence analysis due to gene rearrangement and variable lengths.
  • Manual assembly of IG genes is complex and prone to errors.

Purpose of the Study:

  • To develop a specialized tool, IgBLAST, for efficient and accurate analysis of immunoglobulin sequences.
  • To provide users with detailed insights into IG gene identification, rearrangement junctions, and functional regions.

Main Methods:

  • Development of the IgBLAST sequence analysis tool.
  • Implementation of algorithms to identify germline V, D, and J genes within IG sequences.
  • Integration of batch processing and simultaneous database searching capabilities.

Main Results:

  • IgBLAST accurately identifies germline V, D, and J genes and their rearrangement junctions.
  • The tool delineates IG V domain framework regions and complementarity determining regions.
  • IgBLAST supports both nucleotide and protein sequence analysis and batch processing.

Conclusions:

  • IgBLAST significantly improves the efficiency and accuracy of immunoglobulin sequence analysis.
  • The tool facilitates common tasks in IG sequence analysis, including gene identification and variation assessment.
  • IgBLAST minimizes the risk of missing optimal germline V gene matches through simultaneous database searches.