Monolith NT.115 Instruments

Manufacturer NanoTemper Technologies  |  Available Worldwide
5.0
/
5.0
  |  1 reviews


Product Image
Request Pricing


Turn On Instant Requests

Receive your quote directly from the manufacturer.




Average Rating: 5.0
1 Scientist has reviewed this product

5 out of 5
Ease of use
5 out of 5
After sales service
5 out of 5
Value for money


Rating: 5.0

  • Application Area: Microscale Thermophoresis Detection Of Binding Interactions

"This is a low- to medium-throughput instrument to measure binding constants between two proteins or a protein and a small molecule ligand. The vendor offer two versions: label-based and label-free. Both instrument versions works really well and have consistently produced Kd values close to previously-reported ones or values that end up getting corroborated in the future through traditional calorimetry or SPR techniques. Sample consumption is low and the instrument is very stable (no software crashes or other type breakdown) and easy to use. In our lab, we have used the thermophoresis instruments for over a dozen distinct projects, with results published in almost 10 papers already."

Review date: 12 Oct 2015 | Monolith NT.115 Instruments

Biomolecular interaction studies using the Monolith NT.115: More than binding affinities.

The  Monolith NT.115 measures biomolecular interactions via MicroScale Thermophoresis (MST). It quantifies biomolecular interactions in an easy, rapid and accurate fashion. During an MST experiment, molecules move along a microscopic temperature gradient which is induced by an infrared laser. The molecule of interest will change its migration behavior upon binding to its interaction partner.

Since the directed movement of molecules, termed thermophoresis, does not only depend on the size, but also on the hydration shell and the charge, interactions can be quantified even without an increase in mass or size upon complex formation. The directed movement of molecules across a temperature gradient, termed thermophoresis, does not only depend on size, but also on hydration shell and charge. For this reason, interactions can be quantified even without a significant increase in mass or size upon complex formation.

MST detects binding events between any type of biomolecules, thus offering a large application range, from ions and small molecules to high molecular weight and multi-protein complexes. As MST is conducted without any surface immobilization in free solution, sensitive or bulky molecule assemblies such as liposomes, nanodiscs or membrane proteins can also be studied.

Thermophoresis is detected and quantified using either covalently attached dyes, fluorescent fusion proteins, or intrinsic fluorescence. By combining the precision of fluorescence detection with the flexibility and sensitivity of thermophoresis, Monolith instruments provide a flexible, robust and highly versatile platform to measure molecular interactions.

 

Monolith NT.115 Instruments Benefits:

  • Dynamic range: nM to mM dissociation constants
  • Many commercially available fluorophores and fusion proteins can be used
  • Low sample consumption: just 4 µl per titration point
  • Only 10 nM of the fluorescent molecule is necessary
  • Purification free interaction studies in lysate or serum
  • No size limitation: monitor binding of low MW molecules as well as binding of ribosomes
  • Get your Kd in minutes
  • Kd -Plus: get unique information on sample quality and aggregation along with the Kd
  • Maintenance-free instrument
  • Straightforward handling: simple sample preparation and intuitive software user interface
Industry News
Join the 2nd Drug Discovery Forum
01 Mar 2016

Product Overview

Product Image

Monolith NT.115 Instruments

Manufacturer NanoTemper Technologies  |  Available Worldwide

5.0 / 5.0 | 1 reviews