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Protein characterization, purification, and sequence analysis data for plant-made catfish interleukin 22
Lana Elkins1,2, Maureen C Dolan1,3,2
1Molecular Biosciences Program, United States.
Data in Brief
|January 25, 2021
Summary
Researchers optimized a plant-based system for producing catfish interleukin 22 (cfIL-22). This study details the data and methods used to purify and validate this novel recombinant protein for future applications.
Area of Science:
- Biotechnology
- Molecular Biology
- Protein Expression
Background:
- Plant-based protein production offers a scalable and cost-effective alternative to traditional methods.
- Interleukin 22 (IL-22) plays a crucial role in immune responses, and its production in alternative systems is of significant interest.
Purpose of the Study:
- To present the comprehensive data generated during the optimization of producing and purifying catfish interleukin 22 (cfIL-22) in a plant expression system.
- To provide a detailed workflow for validating plant-produced recombinant proteins.
Main Methods:
- Utilized a plant-based expression platform for recombinant protein production.
- Employed standard workflows including stained protein gels, western immunoblot analyses, DNA/protein sequencing, and computational predictions for post-translational modifications and protein structure.
Main Results:
- Successfully produced and purified a novel catfish interleukin 22 (cfIL-22) using an optimized plant-based protocol.
- Generated extensive datasets including gel electrophoresis, immunoblotting, sequencing, and structural predictions to validate the protein.
Conclusions:
- The data provides a valuable resource for future efforts in expressing other interleukin 22 orthologs.
- This study serves as a guide for optimizing the production and validation of complex animal or human proteins in plant systems.
