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Related Concept Videos

Mass Analyzers: Common Types01:19

Mass Analyzers: Common Types

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The quadrupole mass analyzer consists of four cylindrical metal rods arranged in a diamond carrying a DC voltage and a radio-frequency AC voltage. The motion of ions through the quadrupole depends on the field strength, causing only ions of a certain m/z to resonate successfully and strike the detector at a given field strength. Though the transmission rate for these analyzers is high, the exact elemental composition of the sample is not determined because of low resolution; however, they are...
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Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
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Related Experiment Video

Updated: May 10, 2025

An HS-MRM Assay for the Quantification of Host-cell Proteins in Protein Biopharmaceuticals by Liquid Chromatography Ion Mobility QTOF Mass Spectrometry
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Rapid assay development for low input targeted proteomics using a versatile linear ion trap.

Ariana E Shannon1,2, Rachael N Teodorescu1, No Joon Song1

  • 1Pelotonia Institute for Immuno-Oncology, The Ohio State University Comprehensive Cancer Center, Columbus, OH, 43210, USA.

Nature Communications
|April 22, 2025
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Summary
This summary is machine-generated.

This study introduces a cost-effective mass spectrometry workflow for targeted proteomics using linear ion traps (LITs). The method enables precise quantification of low-abundance proteins from small samples without high-mass accuracy instruments.

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Mass Spectrometry

Background:

  • High-mass accuracy instruments are typically needed for proteomics on limited cell populations.
  • Triple quadrupoles are limited to targeted proteomics, while linear ion traps (LITs) offer versatility.
  • There is a need for cost-effective, accessible mass spectrometry solutions in research labs.

Purpose of the Study:

  • To describe a workflow for developing targeted proteomics assays from global data-independent acquisition (DIA) measurements using a hybrid quadrupole-LIT instrument.
  • To demonstrate the capability of this workflow for quantifying low-level proteins without high-mass accuracy.
  • To validate the method's performance in complex biological samples.

Main Methods:

  • Utilized a hybrid quadrupole-LIT mass spectrometry instrument.
  • Developed an automated software approach for scheduling parallel reaction monitoring (PRM) assays.
  • Performed global data-independent acquisition (DIA) to generate assay parameters.
  • Quantified low-abundance proteins in a 1 ng background proteome.

Main Results:

  • Achieved consistent quantification across three orders of magnitude in a matched-matrix background.
  • Demonstrated quantitative linearity for low-level proteins like transcription factors and cytokines below two orders of magnitude.
  • Showed consistency between flow cytometry and LIT-based proteomics for T cell subsets from a 1 ng sample.
  • Validated the method without the need for stable isotope-labeled standards.

Conclusions:

  • Hybrid quadrupole-LIT instruments offer a valuable and accessible solution for targeted proteomics.
  • The described workflow enables rapid assay development and sensitive protein quantification from limited samples.
  • This approach expands the accessibility of mass spectrometry for diverse laboratory settings.