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Related Concept Videos

Immunoprecipitation01:20

Immunoprecipitation

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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.
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Inductively coupled plasma–mass spectrometry (ICP–MS) is a highly selective and sensitive technique for accurate elemental analysis. Though the analysis of ICP–MS mass spectra is comparatively straightforward, it is affected by spectroscopic and non-spectroscopic interferences. Spectroscopic interferences arise when the plasma contains ionic species with an m/z value the same as the analyte ion. Spectroscopic interference can be categorized as isobaric, polyatomic ions, and...
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Multiplexed Fluorometric ImmunoAssay Testing Methodology and Troubleshooting
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A Tool to Eliminate IgM Immunoassay Interference.

Alexander Pöhler1, Uwe Wessels2, Roland F Staack2

  • 1Roche Pharma Research & Early Development (pRED), Pharmaceutical Sciences, Bioanalysis & Biomarkers, Roche Innovation Center Munich, Roche Diagnostics GmbH, Nonnenwald 2, 82377, Penzberg, Germany. alexander.poehler@roche.com.

The AAPS Journal
|April 11, 2025
PubMed
Summary
This summary is machine-generated.

A new protease selectively cleaves IgM, improving immunoassays. This method removes rheumatoid factor interference and simplifies IgM isotyping, revealing previously underestimated immune responses in gene therapy studies.

Keywords:
Anti-AAV assayIgM interferenceIgM proteaseImmunoassayRheumatoid factor interference

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Area of Science:

  • Biochemistry
  • Immunology
  • Analytical Chemistry

Background:

  • Immunoassays are crucial for bioanalysis.
  • Rheumatoid factor (RF) and treatment-emergent IgM can interfere with immunoassay results.
  • Accurate quantification of immune responses is essential, particularly in gene therapy studies.

Purpose of the Study:

  • To evaluate a novel IgM-selective protease for bioanalytical applications.
  • To demonstrate the protease's ability to eliminate RF interference and simplify IgM isotyping.
  • To investigate the impact of treatment-emergent IgM on anti-capsid IgG assays.

Main Methods:

  • Utilized a newly developed IgM-selective protease.
  • Applied protease treatment in three distinct bioanalytical scenarios.
  • Analyzed immunoassay results before and after selective IgM digestion.

Main Results:

  • Protease treatment successfully eliminated rheumatoid factor interference.
  • IgM isotyping was significantly simplified following protease application.
  • Selective IgM digestion resolved underestimated immune responses in an anti-capsid IgG assay caused by treatment-emergent IgM.

Conclusions:

  • IgM-selective proteolytic cleavage is a valuable tool for enhancing immunoassay performance.
  • This protease effectively removes common interferences, improving assay accuracy and simplifying complex analyses.
  • The findings highlight the importance of addressing IgM interference in gene therapy immunogenicity assessments.