Bio-molecular Interactions

Biomolecular interactions measurements using MicroScale Thermophoresis (MST) is possible since this technique is sensitive to changes in size, charge and hydration shell. It allows measuring a wide range of biomolecular interactions under close-to-native conditions: Label-Free, immobilizationFree, in any buffer or complex bioliquid.

The NanoTemper monolith NT.115 measures biomolecular interactions via detection of fluorescent dyes or fluorescent fusion proteins. The NT 115 allows measuring every interaction type - ranging from the formation of huge protein complexes to the binding of single metal ions. As there are no prerequisites with respect to the buffer composition, even such complex liquids as serum or lysates can be used for interaction studies.

In addition MST data contain valuable information on aggregation and sample quality in general, making it a tool for rapid optimization of experimental conditions.

The equipment available for use in the Laboratory is listed below:
 

Monolith NT.115

 

Biomolecular interactions measurements using MicroScale Thermophoresis (MST) is possible since this technique is sensitive to changes in size, charge and hydration shell. It allows measuring a wide range of biomolecular interactions under close-to-native conditions: Label-Free, immobilizationFree, in any buffer or complex bioliquid.The NanoTemper monolith NT.115 measures biomolecular interactions via detection of fluorescent dyes or fluorescent fusion proteins. The NT 115 allows measuring every interaction type - ranging from the formation of huge protein complexes to the binding of single metal ions. As there are no prerequisites with respect to the buffer composition, even such complex liquids as serum or lysates can be used for interaction studies.
In addition MST data contain valuable information on aggregation and sample quality in general. making it a tool for rapid optimization of experimental conditions.

 

MicroCal PEAQ-ITC

 

Uses isothermal titration calorimeter,a physical technique used to determine the thermodynamics parameters of interactions in solution.
This device delivers direct measurement of all binding parameters in a single experiment and can analyze weak to high affinity binders, using as little as 10µg sample.