Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Upstream Processing01:27

Upstream Processing

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Establishment and characterization of a novel human ampullary carcinoma cell line derived from a Chinese patient.

BMC cancer·2026
Same author

Dynamic changes in excitability and viability of sporadic and <i>SOD1</i>-related amyotrophic lateral sclerosis iPSC-derived motor neurons.

Frontiers in cell and developmental biology·2026
Same author

Regulating interface electric field to stabilize high-voltage KVPO<sub>4</sub>F positive electrode for sustainable potassium-ion batteries.

Nature communications·2026
Same author

Glutathione S-transferase theta 1 (GSTT1) modulates inflammation in Manila clam (Ruditapes philippinarum) during Perkinsus olseni infection.

International journal of biological macromolecules·2026
Same author

Preventive effect of probiotics on oral mucositis: a correspondence.

International journal of surgery (London, England)·2025
Same author

Fasciculation in limbs serves as the predictor of ALS progression: an ultrasound study.

Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology·2025

Related Experiment Video

Updated: May 18, 2026

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

High-throughput Purification of Affinity-tagged Recombinant Proteins

Published on: August 26, 2012

An automatic refolding apparatus for preparative-scale protein production.

Yanye Feng1, Ming Zhang, Linlin Zhang

  • 1State Key Laboratory of Bioreactor Engineering, School of Biotechnology, East China University of Science and Technology, Shanghai, China.

Plos One
|October 3, 2012
PubMed
Summary

An automated apparatus integrates dilution, dialysis, and on-column refolding for efficient protein recovery from inclusion bodies. This system optimizes protein refolding using a slowly decreasing denaturant concentration method for higher yields of active recombinant proteins.

More Related Videos

The MultiBac Protein Complex Production Platform at the EMBL
13:51

The MultiBac Protein Complex Production Platform at the EMBL

Published on: July 11, 2013

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins
11:14

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins

Published on: January 6, 2017

Related Experiment Videos

Last Updated: May 18, 2026

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

High-throughput Purification of Affinity-tagged Recombinant Proteins

Published on: August 26, 2012

The MultiBac Protein Complex Production Platform at the EMBL
13:51

The MultiBac Protein Complex Production Platform at the EMBL

Published on: July 11, 2013

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins
11:14

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins

Published on: January 6, 2017

Area of Science:

  • Biotechnology
  • Protein Chemistry
  • Biochemistry

Background:

  • Protein refolding is crucial for active recombinant protein production from inclusion bodies.
  • Current methods like dilution and dialysis are time-consuming and require extensive trial-and-error.
  • Automation is needed to streamline and improve the convenience of protein refolding processes.

Purpose of the Study:

  • To develop and demonstrate an automated apparatus integrating multiple protein refolding techniques.
  • To optimize protein refolding using a strategy of slowly decreasing denaturant concentration.
  • To assess the efficiency of the apparatus for recovering active proteins from inclusion bodies.

Main Methods:

  • An automated apparatus was designed to integrate varying dilution, dialysis, and on-column refolding.
  • Five proteins (SDF-1/CXCL12, Trx-ARTN, Trx-IGF1, EGFP, BSA) were refolded using different methods on the apparatus.
  • Protein refolding was optimized using a method of slowly descending denaturants or additives.

Main Results:

  • The automated apparatus successfully integrated dilution, dialysis, and on-column refolding techniques.
  • Optimization using slowly decreasing denaturant concentration yielded higher quantities of native protein.
  • The apparatus demonstrated flexibility in handling different proteins and refolding strategies.

Conclusions:

  • The developed automated refolding apparatus offers a convenient and efficient solution for protein refolding.
  • The strategy of slowly decreasing denaturant concentration is effective for maximizing active protein recovery.
  • This automated system represents a powerful tool for preparative scale recombinant protein production.