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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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Upstream processing represents a critical phase in biomanufacturing, wherein biological systems such as microorganisms, mammalian cells, or insect cells are cultivated to produce therapeutic proteins, vaccines, enzymes, or other biologically derived products. This phase encompasses all steps from the selection and genetic manipulation of the production organism to the cultivation of cells in bioreactors under tightly controlled environmental conditions.Host Selection and Genetic OptimizationThe...

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High-throughput Purification of Affinity-tagged Recombinant Proteins
07:44

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Published on: August 26, 2012

Research Progress Fusion Tags for Recombinant Protein Production.

Jing-Jia Yuan1, Shao-Lei Geng2, Tian-Yun Wang3,2

  • 1School of Life Sciences and Technology, Xinxiang Medical University, Xinxiang, Henan, China.

Biotechnology and Applied Biochemistry
|March 28, 2025
PubMed
Summary

Fusion tags enhance recombinant protein production by improving solubility, stability, and yield. This review covers common and novel fusion tags used in genetic engineering for better protein expression and function.

Keywords:
affinity tagsfusion tagsgene engineeringprotein of interestrecombinant proteins

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Engineering

Background:

  • Recombinant proteins are crucial in various applications but often face challenges in expression, purification, stability, and solubility.
  • Structural characteristics of target proteins can impede successful recombinant production.

Purpose of the Study:

  • To review commonly used fusion tags in recombinant protein production.
  • To summarize the functions of these fusion tags.
  • To highlight novel fusion tags and their potential applications.

Main Methods:

  • Review of scientific literature on recombinant protein production techniques.
  • Analysis of fusion tag strategies for improving protein characteristics.
  • Summary of existing and emerging fusion tag technologies.

Main Results:

  • Fusion tags, when appended to recombinant proteins, can significantly enhance solubility, stability, and yield.
  • Tags can range from short peptides to entire protein domains, aiding in purification and conferring new properties.
  • Both established and novel fusion tags offer diverse solutions to protein production challenges.

Conclusions:

  • Fusion tag technology is essential for overcoming limitations in recombinant protein expression and purification.
  • Strategic use of fusion tags can optimize the production of functional recombinant proteins for diverse applications.
  • Continued development of novel fusion tags promises further advancements in protein engineering.