Monolith NT.115 Instruments

Manufacturer NanoTemper Technologies  |  Available Worldwide
4.9
/
5.0
  |  5 reviews


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Average Rating: 4.9
5 Scientists have reviewed this product

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


The instrument is indispensable for us to complement our SPR kinetic measurements.
Rating: 5.0

  • Application Area: Protein-protein and protein-lipid interaction studies utilizing recombinant proteins.

"For us it is very important that we are able to measure the affinity of protein interactions from small amount of recombinant proteins, which is a big advantage of the Monolith instrument. The fast, cca 15 min assay time for one titration is a great feature too. We are pretty much satisfied with the company's customer care system, which includes free technical assistance, some on-site demos after purchase, and well-organized user meetings. The company provides help (technical materials and test measurements) to ensure good assay conditions for particular problems. The prices for consumables are acceptable. We also characterize protein interactions via surface plasmon resonance or quartz crystal microbalance, and with the Monolith instrument we can complement those measurements under similar, or even the same, conditions (concentration, pH, buffer composition, etc.). Altogether, the NT.117 is a great instrument, which does not compromise value for price."

Review date: 01 Dec 2016 | Monolith NT.115 Instruments
  • Status:

    Reviewer

  • Member since: 2016

  • Organization: amcure GmbH



  • Ease of use
    5 out of 5
    After sales service
    5 out of 5
    Value for money
    5 out of 5
MST made my "affinity days" as a researcher
Rating: 5.0

  • Application Area:Characterization of drug candidates

"Using MST we obtained very convincing data for affinities of small molecules/peptides that were highly reproducible. Experimental set-up is very easy and time-efficient in contrast to some alternative methods. But not only that the technology works reliable, the instruments look extremely aesthetic. Last, but not least, the customer support is engaged and efficient."

Review date: 01 Dec 2016 | Monolith NT.115 Instruments
  • Status:

    Reviewer

  • Member since: 2016

  • Organization: 2bind GmbH



  • Ease of use
    4 out of 5
    After sales service
    5 out of 5
    Value for money
    5 out of 5
Nice tool to study drug-target interactions
Rating: 4.7

  • Application Area:Analysis of drug-target interactions

"Our company 2bind uses this technology to study molecular interactions in terms of basic binding parameters. One major focus is on drug-target interactions. The MST offers information on binding affinity, stoichiometry and thermodynamics. The method works in solution with freedom of buffers (even measurements in sera, lysates are possible). It is rapid and consumes very low sample material due to the clever capillary format. We highly appreciate the integrated quality controls showing 1. unspecific adsorption of molecules to the glass surfaces and 2. aggregation effects of the samples. This essential information helps us to optimize the technical setup and obtain optimal data. The output data are highly comparable to ITC and have a good overlap to surface based methods such as SPR. Overall we love this technology, because the size of the interaction partners does not matter. Hence it is the perfect tool to study drug binding to a target protein. The device itself is robust, only takes very little space and the consumables are affordable. The technical support is very good. Thanks guys for your constant support. We can highly recommend this technology."

Review date: 01 Dec 2016 | Monolith NT.115 Instruments
  • Status:

    Reviewer

  • Member since: 2016

  • Organization: Centre for chemical Biology and Theraeputics, inStem, NCBS



  • Ease of use
    5 out of 5
    After sales service
    5 out of 5
    Value for money
    5 out of 5
Great results, its bread and butter for our lab
Rating: 5.0

  • Application Area:Biomolecular interaction studies

"We use Monolith NT.115 every day for protein and small molecule interaction studies. We developed a single point screen method using this machine, which helps us to screen 100's of compounds every day. Setting up experiments using this machine is very easy and it does not require elaborate training. Consumables are cheap and working cost of the machine is also very low. MO Affinity analysis software is user friendly and using the software is easy and quick."

Review date: 01 Dec 2016 | Monolith NT.115 Instruments
  • Status:

    Reviewer

  • Member since: 2014

  • Organization: NIH, NCATS



  • Ease of use
    5 out of 5
    After sales service
    5 out of 5
    Value for money
    5 out of 5
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
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Product Overview

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Monolith NT.115 Instruments

Manufacturer NanoTemper Technologies  |  Available Worldwide

4.9 / 5.0 | 5 reviews