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Protein Interaction Analysis

Creative Biostructure is capable of satisfying your demands in protein interaction services in any type, with strong expertise, extensive experience, proprietary high throughput screening and affinity ranking technology and powerful equipment in hand. Our protein interaction analysis includes affinity ranking, affinity measurement and kinetics measurement.

The test results are applied in a lot of aspects such as the construction of protein-protein interaction profiling map, the investigation of the influence of sequence diversity, the investigation of side-chain posttranslational modifications and rapid antibody screening.

Common Methods to Analyze Protein-Protein Interactions
While the various methods and approaches to studying protein-protein interactions are too numerous to describe here, the table below and the remainder of this section focuses on common methods to analyze protein-protein interactions and the types of interactions that can be studies using each method.

Service Category Description
Surface Plasmon Resonance (SPR) Thermodenaturation-based;
Measuring binding affinity;
Only requiring small quantities of protein samples;
Good correlations with ITC.
Isothermal Titration Calorimetry (ITC) Thermodenaturation-based;
Detecting the complete thermodynamic parameters including affinity, enthalpy and stoichiometry;
Good correlations with SPR.
Bio-layer Interferometry (BLI) Measuring biomolecular interactions based on the principle of optical interferometry;
Real-time monitoring.
Saturation Transfer Differences (STD) NMR For ligand screening and characterization of protein binding;
Values such as KD, the association and dissociation kinetics can be obtained;
Robust and only requiring small quantities of non-labeled macromolecules.
Mircoscale Thermophoresis (MST) Thermodenaturation-based;
Highly sensitive and no essential limitation on molecule size or molecular weight;
Immobilization-free and label-free.
Fluorescence Resonance Energy Transfer (FRET) For membrane protein interactions detection;
Based on distance-dependent interaction between the fluorescent donor-acceptor pairs;
Spatial distribution and oligomerization analysis.

SPR and BLI are most commonly and popularly used technologies to analyze protein interaction. The following compares the differences in SPR, BLI and traditional techniques GST pull-down and Yeast Two-Hybrid in protein interaction study.

Characters of SPR system:
Principle: SPR biosensors respond in real time to changes in the refractive index resulting from the binding and subsequent separation of two proteins. It requires neither radiochemical nor fluorescent labels.

  • High Throughput
  • High Sensitivity
  • Both Qualitative and Quantitative Analysis
  • Low Requirement for Solution Buffer

Characters of BLI System:
Principle: Optical analytical technique analyzes the interference pattern of white light reflected from two surface: a layer of immobilized protein on the biosensor tip, and an internal reference layer. It is a label free technique.

  • High Throughput
  • High Sensitivity
  • Both Qualitative and Quantitative Analysis
  • Low Requirement for Solution Buffer

Creative Biostructure's Protein Interaction Analysis Services deliver analysis data with high accuracy, reasonable price and high speed. Please contact us for more details.

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References:

  1. Fang Y. Label-free Optical Biosensors in Drug Discovery. 2007. Trends in Bio/Pharmaceutical Industry. 3: 34–8.
  2. Gadella TW. FRET and FLIM techniques. 2008 Elsevier. ISBN 978-0-08-054958-3.
  3. Bellucci M. Protein-Protein Interactions: A tool kit to puzzle out functional networks. 2010. VDM Verlag Dr. Müller. ISBN 978-3-639-31160-0.
  4. E M Phizicky and S Fields. Protein-protein interactions: methods for detection and analysis. 1995. Microbiol Rev. 59(1): 94–123.