Monolith by NanoTemper Technologies

Monolith — the only way to get binding affinities in solution using very minimal sample

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.

Use Monolith as your trusted orthogonal tool to validate binding results or to get a Kd in challenging situations that SPR can’t handle. Monolith works great for countless molecules and buffers so you’re able to tackle the wide variety of projects that come your way.

Rely on Monolith’s versatile capabilities to execute immobilization-free experiments quickly and efficiently. Use Monolith to:

• Validate your SPR results with an immobilization-free method.
• Work with challenging interactions that are difficult for SPR.
• Get binding affinity data for almost any type of molecule including IDPs, membrane proteins, large protein complexes, PROTACS, small molecules or ions.
• Capture mass and size⁠-⁠independent measurements.
• Analyze the binding of purified and crude samples in a myriad of assay buffer formulations and without worrying about interference from buffer additives like detergents.
• Quantify low and high binding affinities, from pM to mM, allowing you to detect strong and weak binders.
• Get more than just a Kd: study binding stoichiometry* and thermodynamic parameters*, assess relative affinities with competition assays, and characterize binding cooperativity*.

*Requires offline data handling, not supported by Monolith software

Monolith X with Spectral Shift and MST technologies

Monolith X is equipped with Spectral Shift and MST technologies and provides you high quality data with little to no assay development.

Monolith with MST technology

Monolith comes with MST and enables you to measure high affinity interactions in the pM range, work label-free, or use GFP-tagged proteins