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Related Concept Videos

Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...

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Related Experiment Video

Updated: Jun 9, 2026

Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli
07:35

Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli

Published on: June 9, 2014

Elastin-like polypeptides as a purification tag for recombinant proteins.

Wafa Hassouneh1, Trine Christensen1, Ashutosh Chilkoti1

  • 1Duke University, Durham, North Carolina.

Current Protocols in Protein Science
|September 4, 2010
PubMed
Summary

This study introduces Inverse Transition Cycling, a cost-effective method using elastin-like polypeptides (ELPs) for recombinant protein purification. This technique simplifies protein isolation without chromatography, offering scalability and multiplexing capabilities.

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Efficient Purification of Elastin-Like Polypeptides (ELPs) from E. coli Using an Organic Solvent-based Extraction and Precipitation Method
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Production of Elastin-like Protein Hydrogels for Encapsulation and Immunostaining of Cells in 3D
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Production of Elastin-like Protein Hydrogels for Encapsulation and Immunostaining of Cells in 3D

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Last Updated: Jun 9, 2026

Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli
07:35

Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli

Published on: June 9, 2014

Efficient Purification of Elastin-Like Polypeptides (ELPs) from E. coli Using an Organic Solvent-based Extraction and Precipitation Method
06:30

Efficient Purification of Elastin-Like Polypeptides (ELPs) from E. coli Using an Organic Solvent-based Extraction and Precipitation Method

Published on: January 9, 2026

Production of Elastin-like Protein Hydrogels for Encapsulation and Immunostaining of Cells in 3D
11:46

Production of Elastin-like Protein Hydrogels for Encapsulation and Immunostaining of Cells in 3D

Published on: May 19, 2018

Area of Science:

  • Biotechnology
  • Protein Chemistry
  • Molecular Biology

Background:

  • Recombinant protein purification is crucial for research and therapeutics.
  • Traditional chromatography methods can be expensive and time-consuming.
  • Developing scalable and cost-effective purification strategies is essential.

Purpose of the Study:

  • To present a novel purification method for recombinant proteins using elastin-like polypeptides (ELPs).
  • To demonstrate the effectiveness of Inverse Transition Cycling (ITC) for protein isolation.
  • To highlight the advantages of ELP-based purification over conventional techniques.

Main Methods:

  • Utilizing elastin-like polypeptides (ELPs) as a fusion tag for recombinant proteins.
  • Exploiting the thermally induced phase transition of ELPs (lower critical solution temperature).
  • Implementing Inverse Transition Cycling (ITC) by alternating between soluble and insoluble ELP-fusion protein states.

Main Results:

  • Successful isolation of recombinant ELP fusion proteins from cell contaminants.
  • Demonstration of a sharp and reversible phase transition of ELP fusion proteins upon heating.
  • Achieved purification without the need for chromatography.

Conclusions:

  • Inverse Transition Cycling offers a simple, cost-effective, and scalable method for recombinant protein purification.
  • ELP-based purification is amenable to multiplexing and avoids complex chromatographic steps.
  • This technique provides a valuable alternative for protein purification in various biotechnological applications.