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.
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.
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.
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