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Related Concept Videos

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 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

Affinity and Avidity

Affinity and Avidity

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...

Cross-reactivity

Cross-reactivity

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Related Experiment Video

Updated: May 5, 2026

Printed Glycan Array: A Sensitive Technique for the Analysis of the Repertoire of Circulating Anti-carbohydrate Antibodies in Small Animals

Printed Glycan Array: A Sensitive Technique for the Analysis of the Repertoire of Circulating Anti-carbohydrate Antibodies in Small Animals

Published on: February 14, 2019

Not all antibodies are equal.

Laurence Booth¹

¹Department of Biochemistry and Molecular Biology; Virginia Commonwealth University; Richmond VA USA.

Cancer Biology & Therapy

|December 10, 2013

Summary

This summary is machine-generated.

Epidermal growth factor receptor (EGFR) is a target in colorectal cancer (CRC). Current biomarkers like EGFR expression levels may not accurately predict patient response to anti-EGFR therapies.

Keywords:

KRAS cetuximab colorectal cancer panitumumab rechallenge

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Last Updated: May 5, 2026

Printed Glycan Array: A Sensitive Technique for the Analysis of the Repertoire of Circulating Anti-carbohydrate Antibodies in Small Animals

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Published on: February 14, 2019

Laboratory Scale Production and Purification of a Therapeutic Antibody

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Published on: January 24, 2017

Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms

Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms

Published on: April 17, 2017

Area of Science:

Oncology
Molecular Biology
Cancer Research

Background:

Epidermal growth factor receptor (EGFR) is a validated therapeutic target in various human cancers, including colorectal cancer (CRC).
EGFR signaling pathways (RAS/RAF/MAPK, STAT, PI3K/AKT) regulate critical cellular processes like proliferation, survival, and angiogenesis.
Current anti-EGFR therapies (cetuximab, panitumumab) show limited efficacy as monotherapy in CRC, with response rates around 10% and disease stabilization at 30%.

Purpose of the Study:

To evaluate the role of EGFR as a therapeutic target in colorectal cancer.
To assess the predictive value of EGFR expression levels for anti-EGFR therapy response in CRC patients.

Main Methods:

Review of existing clinical data and studies on anti-EGFR therapies in colorectal cancer.
Analysis of patient selection criteria based on EGFR expression using immunohistochemistry.

Main Results:

Anti-EGFR antibodies like cetuximab and panitumumab have demonstrated modest efficacy in CRC monotherapy.
Clinical findings suggest that EGFR expression levels, measured by immunohistochemistry, may not reliably predict treatment benefit.

Conclusions:

Despite being a validated target, EGFR's predictive biomarkers for anti-EGFR therapy in CRC require further investigation.
The current reliance on EGFR expression for patient selection may not be optimal for predicting clinical benefit in colorectal cancer treatment.