SPR Applications

Enhanced Surface Plasmon Resonance (E-SPR) high performance biosensors from BiOptix are powerful tools that are capable of providing information on kinetic processes (association and dissociation), binding affinities, analyte concentrations and real-time molecule detection. A wide variety of biomolecular interactions can be monitored including the applications listed below.

Biological Applications

• Protein-small molecule interactions
• Protein-protein interactions
• Antibody-antigen interactions
• Kinetics & affinities
• Affinity maturation
• Epitope binning
• Nucleic acid-protein interactions
• Biomolecule concentration measurements

Application Notes

We have notes on use of the 404pi SPR spectrometer in the following applications. Our application notes come in complete scientific format with data and figures.

Protein – Small Molecule:

• Fragment Screening on the Bioptix 404pi
• Label-Free Detection of Interactions between Low Molecular Weight Compounds and Protein
• Label-Free Detection of Small Molecule-Protein Kinetics
• Measuring kinetic rate constants for small molecule-protein interactions where no regeneration condition can be found using Simulject™

Protein – Protein:

• Understanding Protein-Protein Interactions in a Calcium Sensing System

Antibody – Antigen:

• Immunogenicity Screening Using Surface Plasmon Resonance
• Determination of Affinity Differences Between Protein A or an Anti-IgG Affibody When Binding to Antibodies and Fc-fusion Proteins
• Determination of the Kinetic Rate Constants and Affinity of Prostate-Specific Antigen (PSA) to a Monoclonal Antibody (mAb)

Nucleic Acid – Protein:

• Characterization of Single Stranded Binding Protein’s Nucleic Acid Binding Requirements

Nucleic Acid – Nucleic Acid:

• Real-Time Observation of Oligonucleotide Duplex Formation and Dissociation

Biomolecule Concentration Measurement:

• Label-free Multiplex Detection of miRNA