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Related Concept Videos

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...

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Related Experiment Video

Updated: Jun 28, 2026

Microfluidic On-chip Capture-cycloaddition Reaction to Reversibly Immobilize Small Molecules or Multi-component Structures for Biosensor Applications
14:43

Microfluidic On-chip Capture-cycloaddition Reaction to Reversibly Immobilize Small Molecules or Multi-component Structures for Biosensor Applications

Published on: September 23, 2013

Hapten immobilization for antibody sensing using a dynamic modification protocol.

D R Fry1, D R Bobbitt

  • 1Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR 72701, USA.

Talanta
|October 31, 2008
PubMed
Summary
This summary is machine-generated.

This study presents a novel method for creating optical fiber (OF) sensors using a dynamic modification protocol. This regenerable technique effectively immobilizes hydrophobic molecules for antibody detection, improving sensor performance.

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A Protocol for the Identification of Protein-protein Interactions Based on 15N Metabolic Labeling, Immunoprecipitation, Quantitative Mass Spectrometry and Affinity Modulation

Published on: September 24, 2012

Area of Science:

  • Biomedical Engineering
  • Chemical Sensing
  • Materials Science

Background:

  • Immobilization of biologically active ligands on optical fiber (OF) surfaces is crucial for sensor development but often limited by technique.
  • Existing methods can be susceptible to hydrolysis or diffusion limitations.

Purpose of the Study:

  • To extend the dynamic modification protocol for immobilizing hydrophobic haptens on OF surfaces.
  • To develop a regenerable OF sensor for detecting antibodies specific to 2,4-dinitrophenyl (DNP).

Main Methods:

  • Utilized a dynamic modification protocol to immobilize octadecyl 6-(2,4 dinitrophenyl)aminohexanoic acid on an OF surface.
  • Developed an OF sensor for anti-DNP antibodies.
  • Employed time discrimination to mitigate the effects of nonspecific antibody adsorption.

Main Results:

  • Achieved a limit of detection (LOD) of 0.5 nanomolar for anti-DNP antibodies.
  • Determined an apparent dissociation constant (K(apparent)) of 1.0+/-0.2x10^6.
  • Demonstrated that time discrimination minimizes nonspecific binding, enhancing quantitative capabilities.

Conclusions:

  • The dynamic modification protocol offers a simple, regenerable, and robust method for OF sensor fabrication, particularly for hydrophobic molecules.
  • The developed OF sensor shows promise for sensitive and specific antibody detection.
  • Time discrimination is an effective strategy to overcome challenges posed by nonspecific binding in OF sensing applications.