Monolith

Monolith X

Characterize your most challenging interactions

Overview

Monolith X revolutionizes molecular interaction analysis by measuring binding strength directly in solution— no immobilization required. Effortlessly characterize even the most challenging interactions, including those affected by poor sample quality, protein aggregates, or difficult-to-purify proteins. With ultra-low sample consumption and exceptional versatility, Monolith X delivers fast, reliable insights to accelerate your research.

Study diverse interactions (that are difficult for SPR)

Work with almost any molecule including IDPs, membrane proteins, large protein complexes, PROTACS, receptors, nucleic acids, small molecules and other biomolecules.

Immobilization-free measurement

Perfect orthogonal tool for SPR users. It removes the immobilization bias and helps to confirm your results, identify false positives, or find binding partners that your primary assay missed.

Quantify low and high binding affinities

Measure a broad range of binding affinities, from pM to mM, allowing you to detect strong and weak binders.

All buffers/detergents

Analyze the binding of purified and crude samples without worrying about interference from buffer additives like detergents.

Kd in less than 10mins with minimal sample

Measure the dissociation constant (Kd) in less than 10 minutes, using only 10 μl of target.

Monolith comes with two biophysical modalities — Spectral Shift and MST and provides you high quality data with little to no assay development. Simply label one molecule with a fluorophore* and mix it with a dilution series of the binding partner. Load the samples into capillaries, place them in the instrument.
*Alternatively, the intrinsic fluorescence of tryptophan can be used for MST.

Spectral Shift

To evaluate interactions

Monolith X delivers precise spectral shift detection with dual-wavelength measurement at 650 nm and 670 nm in a stable, isothermal environment. By plotting fluorescence intensity ratios against binding partner concentration, it provides accurate Kd calculations, ensuring reliable insights into molecular interactions.

MST

To understand aggregation

Monolith X leverages MicroScale Thermophoresis (MST) to detect ligand binding with ultra-sensitive fluorescence measurements during a precisely controlled, laser-induced temperature shift. By plotting fluorescence changes against binding partner concentration, it delivers accurate Kd values, providing deep insights into molecular interactions with minimal sample consumption.