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Related Concept Videos

Antibody Structure01:10

Antibody Structure

65.8K
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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Antibody Actions01:26

Antibody Actions

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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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Functional Groups02:45

Functional Groups

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Functional groups are a group of atoms with characteristic properties, which when linked to the carbon skeleton of a molecule, alter the properties of that molecule. For example, the presence of certain functional groups on a molecule will make them hydrophilic, whereas others will make them hydrophobic. These functional groups are an indispensable part of organic chemistry and important components of biological molecules, such as carbohydrates, proteins, lipids, and nucleic acids. Each...
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Functional Groups02:45

Functional Groups

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24.6K
Antibody Structure and Classes01:25

Antibody Structure and Classes

9.4K
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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Functionalism01:11

Functionalism

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William James, John Dewey, and Charles Sanders Peirce were instrumental in founding functional psychology, which draws heavily from Darwin's theory of evolution by natural selection. This theory suggests that individual traits, including behaviors, are adapted to their environments through natural selection. At the heart of functionalism is the concept of adaptation, meaning that a trait enhances an individual's chances of survival and reproduction.
James envisioned psychology's...
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Updated: Feb 14, 2026

A GPC3-targeting Bispecific Antibody, GPC3-S-Fab, with Potent Cytotoxicity
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A GPC3-targeting Bispecific Antibody, GPC3-S-Fab, with Potent Cytotoxicity

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Bispecific Antibody-Functionalized Upconversion Nanoprobe.

Hao He, Christopher B Howard, Yinghui Chen

    Analytical Chemistry
    |February 15, 2018
    PubMed
    Summary
    This summary is machine-generated.

    A new bispecific antibody (BsAb) method rapidly creates upconversion nanoparticle (UCNP) nanoprobes for cancer imaging. This facile approach enhances target binding and specificity, offering a general nanoparticle functionalization strategy.

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    Triplet Fusion Upconversion Nanocapsule Synthesis
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    Area of Science:

    • Nanotechnology
    • Bioconjugation Chemistry
    • Optical Imaging

    Background:

    • Upconversion nanoparticles (UCNPs) are promising optical probes for biological applications.
    • Existing bioconjugation methods for UCNPs lack efficiency, stability, and speed.
    • There is a need for improved antibody modification techniques for UCNP-based diagnostics and imaging.

    Purpose of the Study:

    • To develop a facile, high-yield, and rapid bioconjugation method for UCNPs.
    • To create stable UCNP nanoprobes for specific biomolecular recognition and imaging.
    • To overcome limitations of current antibody modification strategies for nanoparticles.

    Main Methods:

    • Utilized a bispecific antibody (BsAb) engineered to bind both UCNPs and cancer biomarkers.
    • Employed a simple vortexing procedure for BsAb-UCNP nanoprobe formation without chemical reactions.
    • Validated the nanoprobes using ELISA-like assays and fluorescence imaging of cancer cells.

    Main Results:

    • BsAb-UCNP nanoprobes formed within 30 minutes via a simple vortexing method.
    • Achieved up to 54% higher target association compared to traditional UCNP nanoprobes.
    • Demonstrated efficient and specific binding to cancer cells for background-free fluorescence imaging.

    Conclusions:

    • The developed BsAb-based method offers a rapid, stable, and efficient approach for UCNP bioconjugation.
    • This technique enables specific targeting of cancer biomarkers for improved imaging and diagnostics.
    • The method provides a generalizable strategy for functionalizing various nanoparticles for biomolecular targeting.