Characterize your most challenging interactions with Monolith

Monolith measures the broadest range of binding affinities in-solution, using very little sample.

Measure high and low affinities in the same instrument

Different projects have different demands. It’s inevitable that you’ll need to look at both weak and strong molecular interactions. With a broad sensitivity range, Monolith measures K_ds varying from pM to mM, so you can tackle as many projects as you want.

Characterize binding events with very little sample

It’s not easy to prepare the large volumes of highly concentrated target and ligand required by ITC. With Monolith, you get a K_d in a fraction of the volume and concentration, leaving you with more sample for additional experiments.

Measure in solution, in close-to-native conditions

Immobilizing molecules in SPR assays often causes them to lose activity, and you’re left without results. Because Monolith measures in solution in most buffers, both binding partners are free to interact in their native conformation, you’ll finally get results.

Characterize interactions with many different types of molecules or samples

You know what types of interactions you need to characterize now, but it’s always difficult to predict what you’ll need to look at in the future. Monolith gives you one less thing to worry about because it has the flexibility to handle all different types of molecules and samples.

Proteins
Membrane proteins, intrinsically disordered proteins (IDPs), receptors, enzymes, antibodies, and nanobodies

Small molecules
Fragments, PROTACs, ions, nanoparticles, peptides, and carbohydrates

Nucleic acids
DNA, RNA, and aptamers

Vesicles
Exosomes and liposomes

Platelets and whole cells

Virus particles and empty capsids