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Antibody Structure

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

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...

Labeling DNA Probes

Labeling DNA Probes

DNA probes are fragments of DNA labeled with a reporter tag to enable their detection or purification. The resulting labeled DNA probes can then hybridize to target nucleic acid sequences through complementary base-pairing, and may be used to recover or identify these regions.
Radioisotopes, fluorophores, or small molecule binding partners like biotin or digoxigenin, are the most widely used reporter tags for labeling DNA probes. These labels can be attached to the probe DNA molecule via...

Single-Strand DNA Binding Proteins

Single-Strand DNA Binding Proteins

For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...

Antibody Structure and Classes

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.

Antibody Actions

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...

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Related Experiment Video

Updated: Jul 22, 2026

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Published on: March 24, 2017

Recognition properties of a sequence-specific DNA binding antibody

J F LeBlanc¹, K E McLane, P W Parren

¹Department of Immunology, The Scripps Research Institute, La Jolla, California 92037, USA.

|May 23, 1998

Summary

This study characterized a novel DNA-binding antibody, Fab-E box, revealing its binding kinetics and specificity determinants. The antibody recognizes extended DNA sequences beyond the canonical E box, with altered dissociation rates influencing its affinity.

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Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

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DNA Sequence Recognition by DNA Primase Using High-Throughput Primase Profiling

DNA Sequence Recognition by DNA Primase Using High-Throughput Primase Profiling

Published on: October 8, 2019

Area of Science:

Molecular Biology
Protein Engineering
Biochemistry

Background:

A recombinant antibody, Fab-E box, was engineered using a transcription factor TFEB alpha-helix.
Fab-E box binds the TFEB E box DNA sequence (CACGTG) with lower affinity than TFEB.

Purpose of the Study:

To determine the precise kinetics of Fab-E box-DNA interaction.
To identify additional DNA target sites and specificity determinants for Fab-E box.

Main Methods:

Kinetic analysis of antibody-DNA interaction.
DNase I protection assays to map binding sites.
Identification of consensus binding sequences.

Main Results:

Fab-E box exhibits a higher dissociation rate compared to TFEB, explaining its lower affinity for E box DNA.
DNase I assays revealed interaction with an E box half-site and identified new binding sites.
A consensus binding sequence (YNYYCAWW) was determined, indicating recognition beyond the E box half-site.

Conclusions:

The DNA binding determinants for Fab-E box are more extensive than initially thought, including preferences for pyrimidines and A+T-rich regions.
Understanding these determinants is crucial for optimizing high-affinity DNA binding by engineered antibodies.