60% Complete

Clear Filters

Showing results {{main.showingResults.from}}-{{main.showingResults.to}} of {{main.totalCount}}

Surface plasmon resonance (SPR) is a label-free detection method that facilitates the real-time analysis of biomolecular interactions. Label-free technologies such as SPR allow scientists to explore biomolecules in their native forms. SPR is a phenomenon that occurs when polarized light strikes an electrically conducting surface at the interface between two media. This generates electron charge density waves called plasmons, reducing the intensity of reflected light at a specific angle known as the resonance angle, in proportion to the mass on a sensor surface.

During typical SPR experiments, a ligand, or binding partner, gets coupled to the surface of an SPR sensor chip. A solution containing the analyte then flows over the sensor surface. As the two biomolecules interact, they cause a change in mass on the sensor surface, which then affects the reflected light. Changes in the light are detected and plotted in a sensorgram.

SPR technology is suitable for detecting interactions between various biomolecules, including antibodies or other proteins, lipids, and nucleic acids. It can also be used for drug candidate screening.

Applications of SPR systems

Here are some main applications of SPR. Click the links to find articles, case studies, and other resources about each application.

Biacore™ SPR systems

Biacore™ systems provide valuable information from high-quality molecular interaction data in a range of fields: from biological research, biotherapeutics and small-molecule drug discovery and development, through immunogenicity studies and vaccine development to quality control. The sensitivity and performance of Biacore™ SPR systems enables detailed characterization of molecular interactions even for challenging targets such as membrane proteins. Use these systems to:

  • Understand the relationship between molecular interaction and function
  • Screen and characterize for hits and optimize leads based on selectivity, affinity, and kinetics
  • Study interactions of ions, small molecules, and multidomain proteins or viruses with targets
  • Screen and characterize antibodies and proteins based on yes/no binding, affinity, and kinetics from the fastest on-rates to the slowest off-rates
  • Quantitate protein by measuring the concentration of active protein with retained biological function
  • Validate results from other techniques/approaches such as ELISA, HTS, or other biophysical methods.

Click to learn more about getting started with SPR. You can also optimize your assay parameters and verify affinity and kinetics constants with our sensorgram simulation tool.

SPR systems FAQs

Below are some answers to frequently asked questions about SPR systems:

What is an SPR system?

These are automated systems that facilitate SPR analysis and capture and produce SPR data.

What do SPR systems do?

They enable the label-free detection of biomolecular interactions in real time.

Which SPR system is right for my application?

We offer Biacore™ systems for a range of scales, including:

  • Biacore™ 8K SPR system: This is a high-throughput system with high sensitivity. It allows efficient characterization and protein optimization of small molecules.
  • Biacore™ S200: Our most selective SPR sensor; facilitates increased productivity.
  • Biacore™ T200: Biacore T200 is a versatile SPR automated system for analyzing molecular interactions.
  • Biacore™ X100: This is a small-scale system for interaction analysis.