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Related Experiment Video

Updated: Jun 25, 2026

Intracellular Refolding Assay
07:18

Intracellular Refolding Assay

Published on: January 24, 2012

An improved method for refolding recombinant decay accelerating factor for therapeutic studies.

Jiang Xu1, Yongliang Hu, Meiliang Gong

  • 1Department of Neurology, Tangdu Hospital, The Fourth Military Medical University, Xi'An, China.

Protein Expression and Purification
|March 4, 2009
PubMed
Summary

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This study presents an improved method for refolding Decay Accelerating Factor (DAF), a promising therapeutic protein. The new procedure efficiently produces active recombinant DAF from inclusion bodies without expensive additives, enabling large-scale production for clinical studies.

Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Immunology

Background:

  • Decay Accelerating Factor (DAF) is a crucial complement regulatory protein with significant therapeutic potential.
  • Current methods for producing recombinant DAF can be inefficient or costly.

Purpose of the Study:

  • To develop an improved and cost-effective procedure for refolding over-expressed rat and human Decay Accelerating Factor (DAF).
  • To enable large-scale production of soluble, active recombinant DAF for therapeutic research.

Main Methods:

  • Over-expression of rat and human DAF in Escherichia coli.
  • Development of a novel refolding protocol for inclusion bodies.
  • Assessment of protein refolding yield and biological activity.

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Related Experiment Videos

Last Updated: Jun 25, 2026

Intracellular Refolding Assay
07:18

Intracellular Refolding Assay

Published on: January 24, 2012

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
14:25

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain

Published on: December 12, 2017

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

High-throughput Purification of Affinity-tagged Recombinant Proteins

Published on: August 26, 2012

Main Results:

  • Achieved 50-70% refolding yield of soluble, active DAF from inclusion bodies.
  • The improved method successfully refolded both rat and human DAF.
  • The protocol avoids the use of expensive L-arginine.

Conclusions:

  • The developed refolding procedure is efficient and cost-effective for producing recombinant DAF.
  • This method facilitates the large-scale preparation of DAF for extensive therapeutic studies.
  • The findings support the clinical application of DAF.