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

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...
Production of Pharmaceuticals01:30

Production of Pharmaceuticals

Industrial insulin production uses genetically engineered E. coli expressing a proinsulin gene controlled by a tryptophan promoter and containing a methionine linker for later cleavage. The cells also carry ampicillin resistance for selective growth. Seed cultures are stored at −80 °C and production begins by thawing a small amount to inoculate starter cultures, which are progressively scaled to a 50,000-L bioreactor. In the bioreactor, E. coli grow in nutrient-rich media under sterile, tightly...
Coordination of Gene Expression Processes in Bacteria01:29

Coordination of Gene Expression Processes in Bacteria

The DNA replication, transcription, and translation processes are intricately coupled in bacteria, allowing efficient gene expression and rapid protein synthesis. While this physical and functional coordination is advantageous, it introduces challenges that bacteria overcome through specific regulatory mechanisms.Coupling of Replication, Transcription, and TranslationThe coupling of replication, transcription, and translation is a hallmark of bacterial gene expression. As the replisome unwinds...

You might also read

Related Articles

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

Sort by
Same author

A screening pipeline to characterize stress-induced enzymes uncovers a cellular function for the poorly characterized alcohol dehydrogenase Bdh2.

Journal of cell science·2026
Same author

Depletion of TECPR2 leads to mitochondrial failure associated with neurodegeneration.

Autophagy·2026
Same author

Complete biosynthesis of psychedelic tryptamines from three kingdoms in plants.

Science advances·2026
Same author

Supramolecular Biopolymer Composed of a Doubly (His)<sub>6</sub>-Tagged Tandem Z-Domain Conjugated by Zn<sup>2<b>+</b></sup> Ions.

ACS synthetic biology·2026
Same author

A pharmacological modality to sequester homomeric proteins.

Nature chemical biology·2026
Same author

DNA methylation shapes transcription factor binding beyond canonical CpG contexts.

Proceedings of the National Academy of Sciences of the United States of America·2025

Related Experiment Video

Updated: May 28, 2026

Generic Protocol for Optimization of Heterologous Protein Production Using Automated Microbioreactor Technology
06:24

Generic Protocol for Optimization of Heterologous Protein Production Using Automated Microbioreactor Technology

Published on: December 15, 2017

Resolving bottlenecks for recombinant protein expression in E. coli.

Yoav Peleg1, Tamar Unger

  • 1Israel Structural Proteomics Center, Faculty of Biochemistry, Weizmann Institute of Science, Meyer Building, Rehovot, Israel. yoav.peleg@weizmann.ac.il

Methods in Molecular Biology (Clifton, N.J.)
|October 4, 2011
PubMed
Summary
This summary is machine-generated.

Escherichia coli (E. coli) is a common system for producing recombinant proteins, but achieving high yields of correctly folded eukaryotic proteins remains difficult. This chapter details strategies for creating expression vectors and enhancing protein solubility in E. coli.

More Related Videos

Optimized Production and Analysis of Recombinant Protein-Filled Vesicles from E. coli
05:19

Optimized Production and Analysis of Recombinant Protein-Filled Vesicles from E. coli

Published on: June 30, 2023

Recombinant Protein Expression for Structural Biology in HEK 293F Suspension Cells: A Novel and Accessible Approach
11:20

Recombinant Protein Expression for Structural Biology in HEK 293F Suspension Cells: A Novel and Accessible Approach

Published on: October 16, 2014

Related Experiment Videos

Last Updated: May 28, 2026

Generic Protocol for Optimization of Heterologous Protein Production Using Automated Microbioreactor Technology
06:24

Generic Protocol for Optimization of Heterologous Protein Production Using Automated Microbioreactor Technology

Published on: December 15, 2017

Optimized Production and Analysis of Recombinant Protein-Filled Vesicles from E. coli
05:19

Optimized Production and Analysis of Recombinant Protein-Filled Vesicles from E. coli

Published on: June 30, 2023

Recombinant Protein Expression for Structural Biology in HEK 293F Suspension Cells: A Novel and Accessible Approach
11:20

Recombinant Protein Expression for Structural Biology in HEK 293F Suspension Cells: A Novel and Accessible Approach

Published on: October 16, 2014

Area of Science:

  • Molecular Biology
  • Biotechnology
  • Protein Expression Systems

Background:

  • Escherichia coli (E. coli) is a widely utilized host for recombinant protein production.
  • Significant advancements have been made in E. coli protein expression over decades.
  • Challenges persist, particularly in producing soluble, correctly folded eukaryotic proteins.

Purpose of the Study:

  • To outline strategies for constructing expression vectors for recombinant protein production.
  • To provide guidelines for improving the solubility of recombinant proteins in E. coli.
  • To address the persistent challenges in high-yield, soluble protein production.

Main Methods:

  • Focus on the design and creation of expression vectors.
  • Exploration of various strategies to enhance protein solubility.
  • Review of established and novel techniques for protein expression optimization.

Main Results:

  • Detailed discussion on vector design principles.
  • Presentation of methods to increase recombinant protein yield and solubility.
  • Identification of key factors influencing protein folding and solubility in E. coli.

Conclusions:

  • Effective vector design is crucial for successful recombinant protein production.
  • Implementing specific strategies can significantly improve protein solubility and yield.
  • Continued research and application of these methods are vital for advancing protein biotechnology.