Related Experiment Video
Updated: Jun 8, 2026
08:08
Quantitative Mass Spectrometric Profiling of Cancer-cell Proteomes Derived From Liquid and Solid Tumors
Published on: February 27, 2015
Handling of solid brain tumor tissue for protein analysis
Christer Ericsson1, Monica Nistér
1Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden. christer.ericsson@ki.se
Methods in Molecular Biology (Clifton, N.J.)
|October 16, 2010
Summary
For optimal protein analysis, handle unfixed brain tumor tissue sterilely on ice for up to 8 hours. This method preserves morphology, immunoreactivity, and protein integrity for both pathological and protein analysis.
Area of Science:
- Neuroscience
- Biochemistry
- Pathology
Background:
- Optimal protein analysis necessitates the use of unfixed tissue samples.
- Preserving protein integrity in brain tumor tissues is crucial for accurate downstream analysis.
Purpose of the Study:
- To establish a simple protocol for handling brain tumor tissue to maintain sample integrity for protein analysis.
- To determine the feasibility of using the same sample for both pathological and protein analysis.
Main Methods:
- Brain tumor tissue samples were handled sterilely and maintained on ice.
- Processing was performed within an 8-hour window.
- Morphology, immunoreactivity, protein integrity, and protein phosphorylation were assessed.
Main Results:
- The proposed handling protocol maintained intact morphology.
- Immunoreactivity and protein integrity were preserved.
- Protein phosphorylation levels were maintained according to established criteria.
- The protocol allows for combined pathological and protein analysis from the same sample.
Conclusions:
- A simple, cold-chain protocol (≤8 hours) is effective for preserving brain tumor tissue for protein analysis.
- This method ensures the integrity of morphology, immunoreactivity, and protein phosphorylation.
- Combined pathological and protein analysis from a single tissue sample is achievable.
