Related Experiment Video
Updated: May 10, 2026

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
Published on: March 4, 2017
The impact of pre-analytical conditions on the serum proteome: heat-stabilization versus nitrogen storage
Timo Gemoll1, Oliver Löwe, Mats Borén
1Section for Translational Surgical Oncology and Biobanking, Department of Surgery, University of Lübeck and University Medical Center Schleswig-Holstein, Campus Lübeck, Germany. Gemoll@chirurgie.uni-luebeck.de
Context:
Biological material reflecting the in vivo composition of markers provides a high potential for biomarker discovery.
Objective:
We compared the serum proteome following heat- and nitrogen-preservation, with and without subsequent storage at room temperature.
Materials And Methods:
Serum samples were collected, treated and analysed by two-dimensional gel electrophoresis. Protein spots were identified and confirmed by two mass spectrometry approaches (MALDI & ESI) and subjected to Ingenuity Pathway Analysis.
Results:
We revealed 24 differentially expressed proteins (p ≤ 0.05) between nitrogen and heat preservation, and 87 between nitrogen and heat preservation with subsequent storage for 120 h at room-temperature. Mass spectrometry identified 25 polypeptides. Pathway analysis resulted in networks maintaining Cellular Assembly and Organization, Movement and Maintenance.
Conclusion:
Heat-stabilization does not substantially change the short-term proteome composition of serum compared with nitrogen treatment. However, heat-stabilization alone seems insufficient for long-term sample preservation for serum samples. We identified transthyretin and apolipoprotein A-IV as sample quality markers.
Related Concept Videos
Protein Denaturation
Bacterial Protein Maturation
