Plant Protein-Protein Interaction Affinity Assay Service

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Plant Protein-Protein Interaction Affinity Assay Service

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Based on surface plasmon resonance (SPR) and biolayer interferometry (BLI), CD BioSciences provides molecular interaction analysis services for clients in plant science research. We assay the affinity of protein, antibody, or Fab fragment interactions to help clients with antibody screening, activity assays, epitope mapping, consistency evaluation, and quality control.

Principles of SPR and BLI

In SPR assays, an interactant is immobilized on a metal film. When the binding partner is added, the refractive index of the film will change characteristically, allowing the interaction between the two materials to be studied.

Schematic diagram of SPR imaging.  Figure 1. Schematic diagram of SPR imaging. (Steiner, G., 2004)

BLI measures macromolecular interactions by analyzing the interference pattern of white light reflected from the surface of the biosensor tip. It is used to determine the kinetics and affinity of molecular interactions.

Schematic diagram of SPR imaging.  Figure 2. Principle of Bio-Layer interferometry (BLI) technology. (Concepcion, J., et al., 2009)

Service Content

Service type Surface plasmon resonance (SPR) Biolayer interferometry (BLI)
Assay program Method development, optimization, and affinity assay.
Assay content
  • Protein-protein interaction detection.
  • Detection of protein binding to small molecules.
  • Antibody–antigen affinity detection.
  • Detection of monoclonal antibody interaction with FcγRs/FcRn/C1q..
  • Affinity/koff ranking.
Special projects Optimization of ligands, analyte concentration interval, and binding or dissociation time. Epitope Binning.
Sample requirements Sample name, type, concentration, molecular weight, labeling, and other information.
Sample concentration > 1mg/mL, purity > 90%. Sample concentration > 0.2mg/mL, purity > 90%, quantity > 100μg.
Analytes are free of high refractive index substances (such as glycerol, sucrose, and imidazole).
No primary amino components in the ligand, such as Tris. 		No amino components in the ligand.

Information We Provide

Whether molecules interact with each other.

Detection of the active content of the target molecule.

Speed of binding and dissociation.

Stability of the complex.

Specificity and selectivity of binding.

Binding strength (affinity) of the two molecules.

Involvement, synergy, and order of assembly in the formation of functional complexes.

Technology Advantages  

Surface Plasmon Resonance (SPR) Biolayer Interferometry (BLI)
  • Real-time monitoring of dynamic processes.
  • Fully automated and highly efficient.
  • Good reproducibility of results.
  • Low sample size and high sensitivity.
  • No purification and labeling required.
  • No labeling required.
  • Real-time measurement of kinetic data.
  • Provides a unique high-throughput platform.
  • Low assay usage.
  • Wide range of applications.

CD BioSciences's research team can provide professional and high-quality protein interaction affinity assay services. We will offer accurate and sensitive instrument platforms, analytical reports, and other lab reports related to data collection and processing procedures. We are committed to providing various analytical expertise to help clients solve technical and analytical-related problems. If you are interested in our services, please contact us for more details.

References

  1. Steiner, G. (2004). Surface plasmon resonance imaging. Anal Bioanal Chem. 379, 328–331.
  2. Concepcion, J., et al. (2009). Label-free detection of biomolecular interactions using BioLayer interferometry for kinetic characterization. Combinatorial chemistry & high throughput screening. 12(8), 791–800.

For research use only, not for clinical use.