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

You might also read

Related Articles

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

Sort by
Same author

Correction to "Cryo-EM Structure of the FtsH Periplasmic Domain Reveals Functional Dynamics".

ACS chemical biology·2026
Same author

Aging, Genetic Susceptibility and Risk of Chronic Inflammatory Upper Airway Diseases: Finding From A Prospective Cohort Study.

Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology·2026
Same author

Purified zymogens reveal mechanisms of snake venom metalloproteinase auto-activation.

eLife·2026
Same author

Establishment of an integrated profiling-fingerprinting-chemometrics strategy for quality control and mechanistic investigation of Fuhuo Capsule.

Journal of chromatography. A·2026
Same author

Fragment-Derived Nicotinic Acid Analogues Inhibit hCA III and Downregulate <i>CA3</i> Expression in HepG2 Cells.

Biomolecules·2026
Same author

Cryo-EM Structure of the FtsH Periplasmic Domain Reveals Functional Dynamics.

ACS chemical biology·2026

Related Experiment Video

Updated: Jun 15, 2026

Production of Recombinant PRMT Proteins using the Baculovirus Expression Vector System
08:57

Production of Recombinant PRMT Proteins using the Baculovirus Expression Vector System

Published on: July 17, 2021

New baculovirus expression tools for recombinant protein complex production.

Simon Trowitzsch1, Christoph Bieniossek, Yan Nie

  • 1European Molecular Biology Laboratory (EMBL), Grenoble Outstation, and Unit of Virus Host Cell Interactions UVHCI, UMI3265, 6 rue Jules Horowitz, Grenoble Cedex 9, France.

Journal of Structural Biology
|February 25, 2010
PubMed
Summary

Producing large protein complexes for research is challenging. We developed the MultiBac system to streamline recombinant protein production and diversification in insect cells, simplifying structural studies.

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

Transient Expression of Foreign Genes in Insect Cells (sf9) for Protein Functional Assay
11:12

Transient Expression of Foreign Genes in Insect Cells (sf9) for Protein Functional Assay

Published on: February 22, 2018

Related Experiment Videos

Last Updated: Jun 15, 2026

Production of Recombinant PRMT Proteins using the Baculovirus Expression Vector System
08:57

Production of Recombinant PRMT Proteins using the Baculovirus Expression Vector System

Published on: July 17, 2021

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

Transient Expression of Foreign Genes in Insect Cells (sf9) for Protein Functional Assay
11:12

Transient Expression of Foreign Genes in Insect Cells (sf9) for Protein Functional Assay

Published on: February 22, 2018

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Eukaryotic proteins often function as large, multicomponent assemblies.
  • Low native abundance of these molecular machines hinders purification and structural analysis.
  • Heterologous overproduction is crucial for high-resolution structure determination.

Purpose of the Study:

  • To present technologies for streamlining recombinant multiprotein complex production.
  • To review developments in the MultiBac baculovirus/insect cell expression system.
  • To detail improvements in baculovirus expression system performance for complex protein production.

Main Methods:

  • Utilized the MultiBac baculovirus/insect cell expression system.
  • Developed robotic routines for automated multigene vector generation.
  • Modified transfer plasmids and generated composite multigene baculoviral DNA.

Main Results:

  • Streamlined the complex production and diversification process for multiprotein complexes.
  • Achieved parallelization and automation of gene assembly for protein complex expression.
  • Introduced simplified and standardized expression procedures using the MultiBac system.

Conclusions:

  • The developed technologies facilitate efficient recombinant multiprotein complex production.
  • Improvements to the MultiBac system enhance baculovirus expression performance.
  • These advancements aid in the structural and functional studies of challenging protein assemblies.