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Updated: May 5, 2026
11:42
High Yield Expression of Recombinant Human Proteins with the Transient Transfection of HEK293 Cells in Suspension
Published on: December 28, 2015
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Glycoprotein Preparation by Heterologous Expression
Koichi Kato1,2, Saeko Yanaka3,4, Hirokazu Yagi3,4
1Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, Okazaki, Japan. kkatonmr@ims.ac.jp.
Methods in Molecular Biology (Clifton, N.J.)
|August 1, 2025
Summary
Stable isotope labeling of glycoproteins is advancing with cost-effective methods. This study details expressing labeled immunoglobulin G using Chinese hamster ovary cells and silkworms.
Area of Science:
- Biotechnology
- Proteomics
- Glycobiology
Background:
- Eukaryotic expression systems, particularly mammalian cells, are standard for stable isotope labeling of glycoproteins.
- Recent advancements aim to lower costs, control glycoforms, and utilize alternative expression systems.
Purpose of the Study:
- To describe procedures for expressing isotope-labeled immunoglobulin G (IgG).
- To evaluate Chinese hamster ovary (CHO) cells and silkworms as expression systems for labeled IgG.
Main Methods:
- Utilized Chinese hamster ovary cells for eukaryotic expression.
- Employed silkworms as an alternative expression system.
- Focused on stable isotope labeling of immunoglobulin G.
Main Results:
- Successfully expressed isotope-labeled immunoglobulin G using both CHO cells and silkworms.
- Demonstrated the feasibility of these systems for producing labeled IgG.
Conclusions:
- Chinese hamster ovary cells and silkworms are viable systems for producing isotope-labeled immunoglobulin G.
- These methods offer alternatives for glycoprotein labeling in proteomics and biopharmaceutical research.
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