Monolith - Molecular Interactions Analyzer

Directly measure the strength of molecular interactions in solution, without the need for immobilization. Characterize nearly all types of molecular interactions - even the most challenging ones. With ultra-low sample consumption and versatile capabilities, Monolith is the best solution for your binding affinity experiments.

With Monolith X, you'll get Spectral Shift and MST - two biophysical modalities to help cover all the types of interactions you encounter. You'll enjoy high-quality results without spending your time on assay development and finally perform experiments without worrying about sample aggregation or impurities.

· Immobilization prevents you from getting a Kd
Suboptimal immobilization or regeneration conditions in SPR negatively impact ligand-binding activity. Because Monolith measures binding in-solution under controlled equilibrium conditions, it will help you handle more challenging ligands, like IDPs with complex conformational dynamics.
· You experience non-specific binding between the analyte and matrix
Since SPR doesn't differentiate between binding of an analyte to an immobilized ligand or to the matrix on a sensor, you'll find yourself doing further testing to recognize and avoid non-specific binding. With Monolith, there's no need to test for non-specific binding since measurements are done in solution.
· You're unable to easily resolve high affinity interactions
It's so difficult to assess high affinity interactions using SPR. Why? Because these types of interactions have very slow dissociation rates and since SPR uses this information to derive binding data - getting a result could take forever. With Monolith, binding is measured directly, so you don't have to wait.
· You're dealing with covalent interactions
Studying covalent binders with SPR is very complex. Because Monolith measures interactions in solution, it's easy to measure covalent interactions - there's no need to figure out how to regenerate biosensors.

Monolith comes with two biophysical modalities - Spectral Shift and MST - that help you measure the strength of your molecular interactions. Experiments start by labeling one molecule with a fluorophore, then mixing a fixed amount of it with a dilution series of the binding partner. Samples are then loaded into capillaries and are placed into the instrument for the measurements to start.
Alternatively, the intrinsic fluorescence of tryptophan can be used for MST.

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