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Related Experiment Video

Updated: Jul 25, 2025

Analysis of Histone Antibody Specificity with Peptide Microarrays
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Affi-BAMS™: A Robust Targeted Proteomics Microarray Platform to Measure Histone Post-Translational Modifications.

Ghaith M Hamza1,2, Eric Miele1, Don M Wojchowski2

  • 1Discovery Biology, Discovery Sciences, R&D, AstraZeneca, Boston, MA 02451, USA.

International Journal of Molecular Sciences
|June 28, 2023
PubMed
Summary
This summary is machine-generated.

The Affi-BAMS platform offers a sensitive and precise method for quantifying histone post-translational modifications (PTMs). This technology enables detailed analysis of epigenetic marks crucial for gene expression and chromatin structure.

Keywords:
BAMSMALDI MSPTMshistonesimmunoaffinity peptide captureproteomics

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Epigenetics

Background:

  • Accurate quantification of post-translational modifications (PTMs) is essential for biological and pharmacological research.
  • Histone PTMs play a critical role in regulating chromatin structure and gene expression.

Purpose of the Study:

  • To evaluate the Affi-BAMS™ platform for quantitative analysis of histone PTMs.
  • To demonstrate the platform's capability in resolving complex PTMs on histones H3 and H4.

Main Methods:

  • Utilized the Affi-BAMS™ (epitope-directed affinity bead capture/MALDI MS) platform.
  • Employed H3 and H4 histone peptides and isotopically labeled derivatives for calibration.
  • Analyzed nuclear cellular lysates and MCF7 cell line models.

Main Results:

  • Achieved a dynamic range of >3 orders of magnitude with <5% technical precision (CV).
  • Successfully resolved heterogeneous N-terminal histone PTMs from 100 µg of starting material.
  • Demonstrated monitoring of dynamic histone H3 acetylation and methylation events, including SILAC quantification.

Conclusions:

  • Affi-BAMS™ provides an efficient and effective approach for analyzing dynamic epigenetic histone marks.
  • The platform's multiplexing capacity enhances its utility for PTM analysis.
  • This method is critical for advancing studies on chromatin regulation and gene expression.