Molecular Interaction AnalyzerBy monitoring changes in physical properties such as mass, refractive index, frequency, etc. during intermolecular interactions, label free, real-time, and dynamic interaction analysis can be achieved. The main technologies include:

1. Surface Plasmon Resonance (SPR) technology

Principle: Using the change in refractive index on the surface of a metal thin film to cause resonance angle shift and infer molecular binding.

Features: Real time observation of binding/dissociation processes, providing kinetic (binding/dissociation rate) and affinity (equilibrium dissociation constant) data, known as the "gold standard" for molecular interaction detection.

2. Biofilm interference technology (BLI)

Principle: Detecting molecular binding by detecting changes in the interference signal of light on the biofilm layer.

Features: No flow path design, high throughput, high sensitivity, suitable for small molecule detection.

3. Microcalorimetry Technique (MST)

Principle: Analyze interactions by detecting changes in molecular thermal swimming velocity.

Features: Low sample consumption, fast detection speed, suitable for complex solution environments.

Features:

No need to mark: manyMolecular Interaction AnalyzerNo need to label sample molecules, which can maintain the natural activity of biomolecules and avoid the influence of labeling on molecular interactions.

Real time monitoring: It can monitor the binding and dissociation processes between molecules in real time, providing dynamic interaction information such as binding rate constants, dissociation rate constants, etc.

High throughput: Some instruments can support 96 well and 384 well plates, which can simultaneously detect multiple samples in parallel and improve detection efficiency.

Compatible with crude samples: Some instruments can measure analytes in crude, unpurified mixtures such as cell lysate or hybridoma supernatant, reducing the steps of sample pretreatment.