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Updated: Jul 15, 2026
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Enrichment of Extracellular Matrix Proteins from Tissues and Digestion into Peptides for Mass Spectrometry Analysis
Published on: July 23, 2015
Protein extraction from mammalian tissues
1Department of Biomedical Sciences, Florida State University College of Medicine, Tallahassee, USA.
Methods in Molecular Biology (Clifton, N.J.)
|April 10, 2007
Summary
This study presents a mild protocol for extracting clock proteins from mammalian tissues like liver, kidney, and brain. The method uses freezing, thawing, and homogenization, efficiently recovering over 90% of target proteins for Western blotting and co-immunoprecipitation.
Area of Science:
- Biochemistry
- Molecular Biology
- Mammalian Tissue Analysis
Background:
- Protein extraction is crucial for techniques like Western blotting and co-immunoprecipitation (coIP).
- Existing methods may not always be suitable for preserving delicate protein structures required for coIP.
- Clock proteins play vital roles in cellular and physiological processes.
Purpose of the Study:
- To describe a mild and efficient protocol for extracting clock proteins from diverse mammalian tissues.
- To ensure the extracted proteins are suitable for downstream applications such as Western blotting and coIP.
Main Methods:
- Tissue homogenization using a handheld homogenizer.
- A simple protocol involving freezing and thawing cycles.
- Extraction applied to mammalian tissues including liver, kidney, and brain.
Main Results:
- The protocol successfully extracts clock proteins from various mammalian tissues.
- Over 90% of clock proteins are recovered using this method.
- The extraction method is mild enough for subsequent coIP and Western blotting.
Conclusions:
- A robust and efficient protocol for clock protein extraction from mammalian tissues has been established.
- This method facilitates the study of clock proteins using Western blotting and coIP.
- The protocol's mildness preserves protein integrity for sensitive analyses.
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