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

Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

6.6K
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...
6.6K

You might also read

Related Articles

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

Sort by
Same author

One-Pot Synthesis of Functionalized Coumarin Fluorophores Enables Rapid Access to Live-Cell Bioorthogonal Labeling and Microenvironmental Sensing Agents.

Bioconjugate chemistry·2026
Same author

Towards Sustainable Synthesis of Peptide Therapeutics via Tag-Assisted Peptide Synthesis and Aryl Selenoester Aminolysis Ligation.

Journal of the American Chemical Society·2026
Same author

Threonine sulfation: a rare post translational modification in insect adipokinetic hormones.

Scientific reports·2026
Same author

Structural studies of an antinecroptosis viral:human functional heteroamyloid M45:RIPK3 using SSNMR.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

The E3-ome gene-centric compendium reveals the human E3 ligase landscape.

Cell·2026
Same author

Ribosomal Translation and Display Selection of Cyclic Glycopeptides through Genetic Reprogramming.

Journal of the American Chemical Society·2026
Same journal

Gas-Responsive Metal-Organic Frameworks for Adaptive Thermal Energy Storage with Tunable Charge-Discharge Temperatures.

Journal of the American Chemical Society·2026
Same journal

Engineering a Thiamine-Dependent Benzoylformate Decarboxylase for Stereodivergent Radical C(sp<sup>3</sup>)-C(sp<sup>3</sup>) Bond Formation.

Journal of the American Chemical Society·2026
Same journal

Accelerated Directional Proton-Coupled Electron Transfer Enabled by Intrinsic Dipole Field in Biomimetic α-Helical Structure.

Journal of the American Chemical Society·2026
Same journal

Alternating Current-Driven Hydrogen Isotope Labeling of Aliphatic Amines Using 1,3-Propanedithiol as an Efficient Hydrogen Atom Transfer Reagent.

Journal of the American Chemical Society·2026
Same journal

Two-Dimensional van der Waals Polar Metal MoOBr<sub>2</sub>.

Journal of the American Chemical Society·2026
Same journal

Negatively Curved Chiral Bilayer Nanographene.

Journal of the American Chemical Society·2026
See all related articles

Related Experiment Video

Updated: Jun 19, 2025

High-throughput Protein Expression Generator Using a Microfluidic Platform
09:26

High-throughput Protein Expression Generator Using a Microfluidic Platform

Published on: August 23, 2012

11.7K

Expressed Protein Ligation in Flow.

Lucas Kambanis1,2, Anthony Ayoub1,2, Max J Bedding1,2

  • 1School of Chemistry, The University of Sydney, Sydney, NSW 2006, Australia.

Journal of the American Chemical Society
|July 25, 2024
PubMed
Summary
This summary is machine-generated.

A new flow chemistry platform for expressed protein ligation (EPL) enables rapid, efficient synthesis of modified proteins. This technology streamlines the production of complex protein targets for diverse research and industry applications.

More Related Videos

Flow Cytometric Analysis of Bimolecular Fluorescence Complementation: A High Throughput Quantitative Method to Study Protein-protein Interaction
11:11

Flow Cytometric Analysis of Bimolecular Fluorescence Complementation: A High Throughput Quantitative Method to Study Protein-protein Interaction

Published on: August 15, 2013

18.4K
OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

6.7K

Related Experiment Videos

Last Updated: Jun 19, 2025

High-throughput Protein Expression Generator Using a Microfluidic Platform
09:26

High-throughput Protein Expression Generator Using a Microfluidic Platform

Published on: August 23, 2012

11.7K
Flow Cytometric Analysis of Bimolecular Fluorescence Complementation: A High Throughput Quantitative Method to Study Protein-protein Interaction
11:11

Flow Cytometric Analysis of Bimolecular Fluorescence Complementation: A High Throughput Quantitative Method to Study Protein-protein Interaction

Published on: August 15, 2013

18.4K
OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

6.7K

Area of Science:

  • Biochemistry
  • Chemical Engineering
  • Synthetic Biology

Background:

  • Expressed protein ligation (EPL) is a powerful technique for protein modification.
  • Traditional batch processes for EPL can be time-consuming and inefficient.
  • Access to homogeneously modified proteins is crucial for various applications.

Purpose of the Study:

  • To develop a flow chemistry platform for expressed protein ligation (EPL).
  • To demonstrate the efficiency and utility of flow EPL for synthesizing modified proteins.
  • To improve reaction rates and product recovery compared to batch methods.

Main Methods:

  • Development of a continuous flow chemistry system for EPL.
  • Semisynthesis of tick-derived chemokine-binding protein ACA-01 with tyrosine sulfate modifications.
  • In-line flow EPL-photodesulfurization for human β-synuclein modification (phosphorylation).
  • Ligation of recombinant protein fragments with synthetic peptides in flow.

Main Results:

  • Flow EPL achieved efficient ligation with high protein recovery and superior reaction rates.
  • Successfully synthesized full-length, sulfated ACA-01 exhibiting potent chemokine binding.
  • Generated unmodified and phosphorylated human β-synuclein in 90 minutes with high purity.
  • Demonstrated access to tens of milligrams of modified proteins.

Conclusions:

  • Flow EPL is a robust and efficient technology for producing homogeneously modified proteins.
  • This platform significantly improves upon batch processing for protein semisynthesis.
  • Flow EPL offers streamlined access to modified proteins for academic and industrial sectors.