Monolith X
Enhanced Monolith version integrating Spectral Shift with MST to expand measurement capabilities.
-Integrates Spectral Shift technology (detects shifts in emission spectra upon binding) AND MST in one platform.
-Spectral Shift enhances detection sensitivity, especially when MST alone may be challenging or when assay development is difficult.
-Broad applicability to nearly any interaction type, with high-quality binding data and minimal need for assay optimization.
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Description
The Monolith series provides robust Microscale Thermophoresis (MST)-based measurements of molecular binding affinities and interactions in solution without immobilization, enabling researchers to study protein–ligand, protein–protein, nucleic acid–ligand, and other biomolecular interactions using very low sample amounts. The MST principle detects changes in fluorescence induced by a precisely controlled temperature gradient applied to molecules in capillaries, and binding strength (KD) is obtained by plotting normalized fluorescence against ligand concentration.
Monolith X adds breakthrough Spectral Shift capability, which detects small changes in emission spectra due to binding events, complementing MST and often reducing assay development needs — especially valuable for challenging interactions and unstable samples.
Specifications
Technology : Spectral Shift + MST
Time to KD : < ~10 min
Dynamic Range : nM to mM
Detected Molecule Size Range : ~10–10⁷ Da
Sample Volume per Assay : ~10 µL
Samples per Run : Up to 24
Fluorescence Channels : 1 / RED
Temperature Control : 20–40 °C ±0.5 °C
Dimensions : ~36×40×58 cm
Application
Binding affinity measurements for protein–ligand, protein–protein, nucleic acid interactions, and beyond.
Analyze interactions that are difficult or impossible with methods like SPR due to immobilization challenges.
Quantify both weak and strong binders in native-like buffers without complex fluidics.
Validate orthogonal data to complement other biophysical methods.