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

Affinity Chromatography01:03

Affinity Chromatography

Affinity chromatography is a powerful technique extensively utilized for separating and purifying specific biomolecules from complex mixtures. It capitalizes on the highly selective binding between an analyte and its counterpart, such as antibody-antigen interactions. The counterpart is immobilized on the stationary phase, forming an affinity column. The stationary phase typically consists of solid support, such as agarose or porous glass beads, immobilizing the affinity ligand. The mobile...
Size-Exclusion Chromatography01:08

Size-Exclusion Chromatography

In size-exclusion chromatography (SEC), also known as molecular-exclusion or gel-permeation chromatography, molecules are separated based on their sizes. This technique is important for separating large molecules such as polymers and biomolecules. The two classes of micron-sized stationary phases encountered in SEC are silica particles and cross-linked polymer resin beads. Both materials are porous, but their pore sizes vary significantly.
Silica particles offer advantages such as rigidity,...
Capillary Electrophoresis: Applications01:30

Capillary Electrophoresis: Applications

Capillary electrophoretic separations offer various modes, each with unique applications. These modes include capillary zone electrophoresis, capillary gel electrophoresis, capillary array electrophoresis, capillary isoelectric focusing, capillary isotachophoresis, micellar electrokinetic chromatography, and capillary electrochromatography.
Capillary zone electrophoresis (CZE) separates ionic components based on their electrophoretic mobility. It has been used to separate proteins, amino acids,...

You might also read

Related Articles

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

Sort by
Same author

Comparing isotherm parameter determination methods for hydrophobic interaction chromatography.

Journal of chromatography. A·2026
Same author

A Review on Quantitative Process Analytical Technology for Continuous Downstream Processing of Monoclonal Antibodies.

Biotechnology and bioengineering·2025
Same author

Towards Rapid Calibration of Bioprocess Quantification Models Using Single Compound Raman Spectra: A Comparison of Four Approaches.

Biotechnology and bioengineering·2025
Same author

Impact of bioreactor process parameters and yeast biomass on Raman spectra.

Biotechnology progress·2025
Same author

Optimization of multi-column chromatography for capture and polishing at high protein load.

Biotechnology progress·2025
Same author

Enantiopurity by Directed Evolution of Crystal Stabilities and Nonequilibrium Crystallization.

Journal of the American Chemical Society·2025
Same journal

Microfluidic rare cell analysis beyond counting: workflow design from enrichment to multi-omics.

Lab on a chip·2026
Same journal

A sperm racetrack to separate sperm by swim speed.

Lab on a chip·2026
Same journal

Controlled encapsulation and droplet size prediction in two-step microfluidic double emulsions.

Lab on a chip·2026
Same journal

A particulate blood-mimicking fluid with physiological biconcave geometry for microscale hemorheology.

Lab on a chip·2026
Same journal

Multicellular sensor arrays fabricated by capillary stamping for pattern-based odor discrimination.

Lab on a chip·2026
Same journal

A real-time microfluidic surveillance system for multiplex detection of heavy metal contamination in wastewater.

Lab on a chip·2026
See all related articles

Related Experiment Video

Updated: Jun 25, 2026

In-vivo Detection of Protein-protein Interactions on Micro-patterned Surfaces
07:42

In-vivo Detection of Protein-protein Interactions on Micro-patterned Surfaces

Published on: March 19, 2010

Protein self-interaction chromatography on a microchip.

Kedar Deshpande1, Tangir Ahamed, Luuk A M van der Wielen

  • 1Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628BC, Delft, The Netherlands.

Lab on a Chip
|February 5, 2009
PubMed
Summary
This summary is machine-generated.

This study introduces a miniaturized Self-Interaction Chromatography (SIC) method on a microchip to measure protein-protein interactions. This innovation enables faster, more cost-effective protein crystallization screening and rational design.

More Related Videos

A Microfluidic Chip for the Versatile Chemical Analysis of Single Cells
15:41

A Microfluidic Chip for the Versatile Chemical Analysis of Single Cells

Published on: October 15, 2013

A Microfluidic Chip for ICPMS Sample Introduction
11:16

A Microfluidic Chip for ICPMS Sample Introduction

Published on: March 5, 2015

Related Experiment Videos

Last Updated: Jun 25, 2026

In-vivo Detection of Protein-protein Interactions on Micro-patterned Surfaces
07:42

In-vivo Detection of Protein-protein Interactions on Micro-patterned Surfaces

Published on: March 19, 2010

A Microfluidic Chip for the Versatile Chemical Analysis of Single Cells
15:41

A Microfluidic Chip for the Versatile Chemical Analysis of Single Cells

Published on: October 15, 2013

A Microfluidic Chip for ICPMS Sample Introduction
11:16

A Microfluidic Chip for ICPMS Sample Introduction

Published on: March 5, 2015

Area of Science:

  • Biochemistry and Biophysics
  • Microfluidics and Lab-on-a-Chip Technology
  • Protein Crystallization

Background:

  • Protein-protein interactions are crucial for biological functions and understanding protein phase behavior.
  • Self-Interaction Chromatography (SIC) offers a method for quantitative thermodynamic analysis of these interactions.
  • Current methods can be time-consuming and require significant amounts of protein.

Purpose of the Study:

  • To develop a miniaturized, resin-free experimental procedure for measuring protein self-interactions on a microchip.
  • To adapt Self-Interaction Chromatography (SIC) for microfluidic applications.
  • To facilitate rational design of protein crystallization through efficient screening.

Main Methods:

  • Development of a novel microchip-based experimental setup for Self-Interaction Chromatography (SIC).
  • Elimination of traditional chromatographic resins in the microchip procedure.
  • Measurement of protein self-interaction parameters, such as the osmotic second virial coefficient (B22).

Main Results:

  • Successful miniaturization of SIC to a microchip format.
  • Demonstration of resin-free protein self-interaction measurements.
  • Acquisition of quantitative thermodynamic data relevant to protein phase behavior.

Conclusions:

  • The microchip-based SIC is a significant advancement for studying protein-protein interactions.
  • This technology provides a foundation for a microfluidic platform for protein crystallization screening.
  • The method reduces protein consumption and experimental time, lowering costs.