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Updated: May 2, 2026

Author Spotlight: Expression and Purification of Human Solute Carrier Transporters Using Codon-Optimized Genes

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Published on: September 29, 2023

Expression and solubility testing in a high-throughput environment.

Keehwan Kwon¹, Scott N Peterson

¹J. Craig Venter Institute, 9704 Medical Center Drive, Rockville, MD, 20850, USA, kkwon@jcvi.org.

Methods in Molecular Biology (Clifton, N.J.)

|March 5, 2014

Summary

This summary is machine-generated.

This study presents a 96-well platform for efficiently expressing and screening recombinant protein solubility. This method aids high-throughput protein production using the widely adopted E. coli system.

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High Throughput Quantitative Expression Screening and Purification Applied to Recombinant Disulfide-rich Venom Proteins Produced in E. coli

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Published on: July 30, 2014

Area of Science:

Biochemistry
Molecular Biology
Protein Expression

Background:

High-throughput protein production relies on efficient expression and solubility screening.
Escherichia coli (E. coli) is a preferred system for recombinant protein expression due to its adaptability to high-throughput pipelines.

Purpose of the Study:

To develop and describe a novel 96-well platform for recombinant protein expression and solubility screening.
To enhance the efficiency of target protein production in a high-throughput format.

Main Methods:

Utilized a 96-well format for parallel expression of target proteins.
Implemented screening assays to assess protein solubility.
Employed the E. coli expression system for recombinant protein production.

Main Results:

Demonstrated efficient expression of target proteins in the 96-well format.
Successfully screened protein solubility using the developed platform.
Validated the platform's utility for high-throughput protein production pipelines.

Conclusions:

The described 96-well platform facilitates efficient recombinant protein expression and solubility screening.
This approach streamlines high-throughput protein production, particularly within E. coli systems.
The platform offers a valuable tool for researchers involved in protein engineering and structural biology.