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Related Experiment Video

Updated: Jul 3, 2026

Proteomic Profile of EPS-Urine through FASP Digestion and Data-Independent Analysis
14:48

Proteomic Profile of EPS-Urine through FASP Digestion and Data-Independent Analysis

Published on: May 8, 2021

Optimizing sample handling for urinary proteomics.

Richard S Lee1, Flavio Monigatti, Andrew C Briscoe

  • 1Department of Urology, Urological Diseases Research Center, Harvard Medical School and Children's Hospital Boston, Boston, Massachusetts 02115, USA. richard.lee@childrens.harvard.edu

Journal of Proteome Research
|July 30, 2008
PubMed
Summary
This summary is machine-generated.

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Standardizing urinary proteome analysis is crucial for biomarker discovery. This study found that common sample handling methods like protein extraction, room temperature exposure, and freeze-thaw cycles do not significantly alter urinary proteomic data for mass spectrometry.

Area of Science:

  • Biochemistry
  • Proteomics
  • Clinical Diagnostics

Background:

  • Accurate urinary proteome analysis is essential for identifying disease biomarkers.
  • Variations in sample collection and handling can introduce significant measurement discrepancies.
  • Standardized protocols are needed for reliable qualitative and quantitative proteomic measurements.

Purpose of the Study:

  • To evaluate the impact of common laboratory procedures on the urinary proteome.
  • To determine if protein extraction, handling time, and freeze-thaw cycles affect urinary proteomic data integrity.
  • To assess the suitability of urinary samples for mass spectrometry-based biomarker discovery despite these variables.

Main Methods:

  • Investigated the effects of different protein extraction techniques on urinary samples.

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Last Updated: Jul 3, 2026

Proteomic Profile of EPS-Urine through FASP Digestion and Data-Independent Analysis
14:48

Proteomic Profile of EPS-Urine through FASP Digestion and Data-Independent Analysis

Published on: May 8, 2021

Comparative Proteomic Analysis of Whole Kidney, Medulla, and Cortical Tubules in Diabetic Pathogenesis of Kidney Injury in Mice
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  • Assessed the impact of prolonged room temperature handling on sample composition.
  • Examined the consequences of multiple freeze-thaw cycles on urinary proteins and peptides.
  • Utilized mass spectrometry to analyze changes in the urinary proteome.

    • Main Results:

    • The chosen protein extraction methods did not significantly alter the urinary proteome.
    • Handling urinary samples at room temperature for extended periods showed no detrimental effects on proteomic profiles.
    • Repetitive freeze-thaw cycles did not degrade the quality of protein or peptide information.
    • Mass spectrometry analysis confirmed the stability of the urinary proteome under tested conditions.

    Conclusions:

    • Standard laboratory procedures for protein extraction and sample handling, including room temperature exposure and freeze-thaw cycles, appear robust.
    • These findings suggest that variations in these common methods may not significantly compromise the urinary proteome.
    • The urinary proteome remains amenable to analysis by mass spectrometry, supporting its use in biomarker discovery.