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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...

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Related Experiment Video

Updated: Dec 17, 2025

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

[Progress in shark single-domain antibody].

Xing Liu¹, Qi Chen¹

¹College of Food Science and Engineering, Hainan University, Haikou 570228, Hainan, China.

Sheng Wu Gong Cheng Xue Bao = Chinese Journal of Biotechnology

|June 30, 2020

Summary

This summary is machine-generated.

Shark single-domain antibodies (shark VNAR) offer a promising alternative to traditional monoclonal antibodies (mAbs). These miniaturized VNARs possess superior properties like high affinity and tissue penetration for diverse applications.

Keywords:

Selachimorpha immunoglobulin new antigen receptor shark single domain antibody variable domain of immunoglobulin new antigen receptor

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Area of Science:

Biotechnology and Molecular Biology
Immunology
Drug Discovery

Background:

Monoclonal antibodies (mAbs) are crucial in diagnostics and therapeutics but face limitations due to high molecular weight and complex structures.
There is a growing need for advanced antibody alternatives with improved characteristics for broader applications.
Shark variable domain of immunoglobulin new antigen receptor (VNAR) represents a novel class of miniaturized antibodies.

Purpose of the Study:

To review the structural and functional characteristics of shark VNARs.
To explore the generation, humanization, and affinity maturation techniques for VNARs.
To discuss the application fields, advantages, disadvantages, and future prospects of shark VNARs.

Main Methods:

Genetic engineering to derive VNARs from the natural immunoglobulin new antigen receptor (IgNAR) found in sharks.
Comparative analysis of VNAR properties against traditional monoclonal antibodies (mAbs).
Review of existing literature on VNAR generation, optimization, and application.

Main Results:

Shark VNARs are the smallest known antigen-binding domains (12 kDa) in vertebrates.
VNARs exhibit superior qualities including high affinity, stability in harsh environments, good solubility, and enhanced tissue penetration.
VNARs can recognize hidden epitopes inaccessible to larger antibodies.

Conclusions:

Shark VNARs present significant advantages over mAbs, making them highly attractive for immunochemical reagents and drug discovery.
Further development in VNAR technology holds promise for innovative diagnostic and therapeutic solutions.
VNARs are a versatile platform with broad potential across various biomedical fields.