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Immunoprecipitation

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: May 1, 2026

Activated Cross-linked Agarose for the Rapid Development of Affinity Chromatography Resins - Antibody Capture as a Case Study

Activated Cross-linked Agarose for the Rapid Development of Affinity Chromatography Resins - Antibody Capture as a Case Study

Published on: August 16, 2019

Avoiding antibody aggregation during processing: establishing hold times.

Varsha Joshi¹, Tarun Shivach, Vijesh Kumar

¹Department of Chemical Engineering, IIT Delhi, Hauz Khas, New Delhi, India.

Biotechnology Journal

|April 23, 2014

Summary

This summary is machine-generated.

Biotech product aggregation and charge variants impact therapeutic efficacy. This study suggests a modeling approach to establish hold times, finding aggregation occurs at low pH and charge variants at high pH during monoclonal antibody processing.

Keywords:

Aggregation Charged variants Immunoglobulin Regression analysis Stability

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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

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:

Biopharmaceutical manufacturing
Protein aggregation and heterogeneity analysis
Therapeutic antibody development

Background:

Aggregation and charge variants in therapeutic proteins like monoclonal antibodies (mAbs) can lead to immunogenicity, affecting safety and efficacy.
Establishing appropriate hold times for process intermediates is crucial for maintaining product quality during mAb production.

Purpose of the Study:

To propose an empirical modeling and least squares regression approach for determining hold times during mAb intermediate processing.
To analyze aggregation and charge heterogeneity of immunoglobulins under typical downstream processing buffer conditions.

Main Methods:

Analysis of two immunoglobulins using size exclusion chromatography, ion exchange chromatography (IEC), and circular dichroism.
Evaluation of aggregation and charge heterogeneity across various buffer conditions and pH levels relevant to mAb downstream processing.

Main Results:

Aggregation was highest at pH 3 (affinity chromatography buffers), particularly in citrate buffer, and minimal in anion and cation exchange chromatography buffers (pH 6-8).
Charge heterogeneity (acidic and basic variants) showed opposite behavior, with increased susceptibility to degradation at high pH compared to low pH.
Product stability is significantly impacted by routinely used manufacturing conditions.

Conclusions:

The study highlights the critical role of buffer conditions and pH in influencing both aggregation and charge heterogeneity of mAbs.
An empirical modeling approach is proposed to establish process intermediate hold times, ensuring product stability.
Adoption of this approach by manufacturers is recommended to guarantee the quality and safety of therapeutic antibody products.