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Updated: Jun 28, 2026

HeLa Based Cell Free Expression Systems for Expression of Plasmodium Rhoptry Proteins

HeLa Based Cell Free Expression Systems for Expression of Plasmodium Rhoptry Proteins

Published on: June 10, 2015

High-throughput protein expression using cell-free system.

Kalavathy Sitaraman¹, Deb K Chatterjee

¹Protein Expression Laboratory, SAIC-Frederick, Inc., National Cancer Institute at Frederick, MD, USA.

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

|November 7, 2008

Summary

This summary is machine-generated.

Cell-free protein synthesis offers a rapid, efficient alternative to traditional methods. This study presents a high-yield, 96-well plate protocol using E. coli extract for recombinant protein expression.

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Published on: July 31, 2012

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Last Updated: Jun 28, 2026

HeLa Based Cell Free Expression Systems for Expression of Plasmodium Rhoptry Proteins

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Published on: June 10, 2015

From Cells to Cell-Free Protein Synthesis within 24 Hours Using Cell-Free Autoinduction Workflow

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A Convenient and General Expression Platform for the Production of Secreted Proteins from Human Cells

A Convenient and General Expression Platform for the Production of Secreted Proteins from Human Cells

Published on: July 31, 2012

Area of Science:

Biochemistry
Molecular Biology
Proteomics

Background:

Efficient protein synthesis is crucial in the post-genomic era for understanding gene function.
Conventional cell-based expression methods face challenges like low yield, solubility issues, and toxicity.
Structural genomics and functional proteomics require high-throughput production of soluble proteins.

Purpose of the Study:

To address the limitations of cell-based protein expression.
To present a novel, high-yield cell-free protein synthesis protocol.
To facilitate rapid recombinant protein production for research.

Main Methods:

Utilized a cell-free protein synthesis system with E. coli extract.
Employed a batch mode protocol in a standard 96-well plate format.
Focused on optimizing conditions for high-yield recombinant protein expression.

Main Results:

Achieved high yields of recombinant proteins.
Demonstrated the efficiency and scalability of the 96-well plate format.
Successfully expressed proteins that may be toxic or unstable in vivo.

Conclusions:

Cell-free synthesis provides a versatile and efficient alternative for protein production.
The presented protocol enables high-throughput, automated recombinant protein expression.
This method accelerates research in structural genomics and functional proteomics.