Nanotemper provide leading and new gold standard technologies to measure molecular interactions and unfolding events. NanoTemperTech are the sole providers of technologies including MST (Micoscale Thermophoresis), TRIC (Temperature Related intensity changes); Nanotemper also supply key technologies including NanoDSF (differential Scanning Fluorimetry) and DLS (Dynamic Light scatering).
Instruments include: Monolith, Automated Monolith, Dianthus, Prometheus, Prometheus Panta, Tycho
Stefan Duhr and Philipp Baaske set out to build a company to address challenges researchers were facing with the ultimate goal of helping to move science forward.
NanoTemper was started in 2008 after Stefan and Philipp met at Ludwig-Maximilians-University Munich. At the time, the effect of thermophoresis was not known within the Life Sciences community, but Stefan and Philipp knew that it was important. Realizing the shortcomings of current protein research techniques, they came up with a method, MicroScale Thermophoresis that was enormously sensitive, and would bring researchers one step closer to developing better drugs faster. Now, NanoTemper has over 150 employees with representation in 13 countries around the world including Germany, UK, Poland, Denmark, Belgium, Netherlands, Spain, France, USA, Brazil, Russia, China, and India.
Get fast, non-stop, highly sensitive hit screening
Quickly find and rank hits
Dianthus removes the complexity of binding interaction measurements for drug discovery screening. Get the fastest time to meaningful results with no immobilization required, because you demand it.
Find hits for any target type in any buffer or bioliquid
Consume the smallest amount of your target and library compounds
Measure the tightest interactions down to picomolar Kds
Tackle many projects, not just a few
Explore every target, even the most challenging ones
There’s no end to the projects you can do. Study targets of any size or mass — from ions to multimeric proteins — and type — proteins, nucleic acids, saccharides, and more.
Evaluate any sample type in any buffer
Dianthus isn’t picky. Feel free to prep your target in the buffer that ensures its stability and integrity. Even use lysates or bioliquids without diluting them.
Measure affinities with the highest sensitivity
Whether strong or weak, Dianthus detects a wide range of binding affinities — picomolar to millimolar — so you don’t have to use other methods.
Characterize in solution, no immobilization required
Analyzing interactions in close-to-native conditions is ideal. Dianthus characterizes in solution, so interfering with your target’s binding site or spending on expensive immobilizing chemistries isn’t an issue.
Consume small amounts of target and compounds
Every little bit counts. Saving on costly sample and library compounds means you can do more screening or use them in other projects.
Get meaningful results faster at any throughput
Dianthus swiftly analyzes 384 data points in 30 minutes and has flexible throughput. Choose to run one sample or as many as you want.
Use Dianthus 24/7
With Dianthus, there’s no fluidics. That means regular maintenance is not required ➡️ which means there’s no downtime ➡️ which means you can use it 24/7 whenever you want. Since Dianthus uses a 384-well microplate format, it’s compatible with many automation solutions and easily fits into your current workflow for even more hands-free time.
Fast time to results and nanomolar sensitivity
Fast time to results with highest picomolar sensitivity
Fastest time to results with highest picomolar sensitivity
Screen for hits and optimize leads based on affinity
Finding true hits faster is the most important step in making your drug discovery workflow efficient. With Dianthus, you’ll find hits quickly and move on to hit validation confidently, whether it’s fragment-based or small molecule single-dose screening.
Spend less time sorting through the strong and weak binders. Dianthus generates easy-to-interpret affinity ranking tables and histograms to help you quickly decide on the right candidates and start lead optimization sooner.
Once validation is complete, it’s time to improve target specificity, selectivity, and potency. Use Dianthus to verify that binding affinities remain strong. This, combined with your ADME, toxicity, and PK/PD results, ensures you’re developing the best drug candidates.
Want to see data from a real application?
Use proven technology that’s been around for over 10 years
Quantifying molecular interactions — measuring how tight or weak a ligand binds to its target — via Temperature Related Intensity Change (TRIC) isn’t new. It’s done by labeling your target molecule with a fluorescent dye and mixing it with your ligand. Then, a very precise and brief laser-induced temperature change is applied, causing a variation in fluorescence intensity which is amplified if your ligand binds to your target. This change in fluorescence is measured and plotted against your ligand concentration to obtain the dissociation constant or Kd.
Decide which hits are worth moving forward with sooner
Generating results is great, but getting automated, actionable insights from your results is even better. Dianthus DI.Screening Analysis software gives you screening summaries as well as easy-to-interpret ranking tables and histograms. Quickly compare Kds and decide which candidates are worth moving forward with sooner rather than later.
Use high-quality consumables for fast hit screening
Get the high quality and consistency you expect from consumables when finding and validating hits. Dianthus 384-well plates have a proprietary coating that prevents protein from sticking to the wells, and they go through rigorous QC testing to ensure consistency from well to well. So, it’s no wonder the plate’s barcode helps you track your assay and data back to a specific plate. You’ll also want to use a 2nd Generation labeling kit — it labels your proteins or peptides with fluorophores selected for their sensitivity to binding events — so you get the best results.
If you’re looking to get your hit screening assay up and running quickly, use the Buffer Exploration Kit. The buffer plate provides a systematic approach to assay development — it’s pre-loaded with buffer systems that contain various salts, detergents, and additives. Simply mix any of these buffer combinations with your sample to quickly find the right buffer conditions. Finally, reduce the time and cost of assay development.
Do more than screening
Little did you know that Dianthus is capable of doing more than just hit ID and validation. Because it handles a wide range of targets and has flexible throughput, it’s so easy to choose Dianthus as your primary tool for characterization of molecular interactions for a variety of applications.
Characterize binding events to understand biological processes and structure-function relationships
Analyze how multimeric proteins, GPCRs or aptamers interact with their ligands
Support and confirm X-ray crystallography and Cryo-EM findings
Perform competition assays in the presence of inhibitors
Find out your protein's quality quickly
Tycho named one of the Top 10 Innovations of 2018 by The Scientist
Protein quality is key to getting consistent results
Most of the time, you don’t know something’s wrong until you’re several steps into your experiment and you see inconsistent results. What if you could simply check the quality of your sample before you even start? That’s where Tycho comes in.
Tycho tells you so much about the quality of your protein
It tells you about presence, purity, concentration, functionality and similarity — in a single experiment. These can all be measured simply by determining whether your protein is structurally intact or properly folded.
Analyze under native conditions
There’s no need to fluorescently label or modify your sample — that means no assay development and only real results.
Get answers in minutes
Generate informative data in just 3 minutes — it makes deciding what to do next that much easier. Watch video
Easily test any protein sample type
Forget dialyzing or doing sample dilutions. Determine the quality of any protein in any type of buffer over a wide range of concentrations.
Save scarce bench space
Tycho’s small footprint doesn’t take up a lot of bench space which means more space for you!
Conserve precious sample
Purifying protein because you’ve run out of sample is like 🤦♂️or 🤦♀️. Not only can checking your protein’s quality help you run less experimental parameters later, but you only need 10 µL of sample.
I put every protein in Tycho first. The data is very reproducible in our hands. Just mix your samples, put the capillaries in and 3 minutes later you have your results. It’s the only equipment I would recommend to anyone working on proteins because there are no downsides in having a Tycho.
Dr. Stefan Gajewski
Scientist I, Nurix Inc., California
Finally get answers to questions you routinely encounter
Are impurities causing these questionable results?
Is this batch of protein the same as the last one?
Were these samples properly stored?
Did the protein lose its functionality?
Was the right amount of material used in the assay?
Is there even any protein in this sample prep? ?
Is the salt, pH or buffer affecting the protein?
Verify protein quality at any step in your workflow
Test for the presence of your protein
Pinpoint the fraction that contains your isolated protein and check its functionality
Confirm batch similarity, purity, functionality and concentration
Determine the right buffer storage conditions. After thawing, compare similarity, purity, functionality and concentration to data obtained before storage.
Check the concentration of your protein and test if it’s functional or has activity
Are you working with Surface Plasmon Resonance (SPR)?
Make your SPR workflow smoother, more efficient, and less costly with Tycho.
Measure many sample types
Virus-like particles (VLPs)/Capsids
Functionalized proteins (mAbs)
Use Tycho for your practical everyday applications
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Identify optimal storage conditions for fridge, freezer, or -80 °C
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Confirm sample quality of crystals before x-ray crystallography experiments
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Ensure samples are of the right quality for NMR experiments
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Monitor the presence of your protein during any purification step
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Check quality of samples prior to cryo-EM
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Determine how much protein is isolated and its concentration
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Examine binding interactions, quick and label-free
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Monitor impact of salts, pH and ions when developing or testing buffer recipes
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Gain quick insights on protein quality to assist in assay development
Tycho NT.6 was adopted by all our lab members in no time, providing crucial quality information not detectable before. It will become a standard tool for everyone working on protein biochemistry.
Dr. Gregor Witte
Principal Investigator, K.P. Hopfner lab, Ludwig-Maximilians-University of Munich
How does Tycho identify sample quality?
Tycho verifies protein quality by looking at the structural integrity (or foldedness) of a protein. As a thermal ramp is applied, the changes in the intrinsic fluorescence, detected at both 350 nm and 330 nm, from tryptophan and tyrosine residues in the protein are measured. These changes in fluorescence signal indicate transitions in the folding state of a protein. The temperature at which a transition occurs is called the inflection temperature (Ti). The fluorescence is recorded during the thermal run, plotted as ratio and used to calculate Ti. Its initial value along with the change in signal over the run (Δ ratio) is also recorded.
Verify the quality of your starting material or similarity between batches
With Tycho, compare the structural integrity or unfolding profile of that new sample prep to your reference sample of the right quality to verify they are similar. If they differ, you may have a sample of lower quality that contains contaminants—this indicates the need to further purify it or optimize your purification workflow. Having confidence that you are working with the highest quality samples all the time, will result in more consistent results.
Want to get more technical?
Check for sample presence, amount and purity
Once you’ve run Tycho to confirm results from traditional methods, you’ll realize that the results from Tycho not only show you the presence of your protein but also if impurities are present. And, it even lets you determine the concentration of it. So in the future, shelve those traditional methods that take time and use up a lot of your precious material.
Precise and Concentration
Determine the right buffer recipe for storage or assay development
Use Tycho to identify the right buffer recipe for storage or assay development to preserve the quality of your protein. Quickly screen different buffers, additives and excipients as well as storage temperatures and time periods to determine the right conditions for your protein samples. Use this information to help optimize your assay conditions for future experiments. In the end, you’ll spend less time generating unnecessary batches of protein.
Monitor Storage Conditions
Quickly confirm functionality
Tycho tests functionality in 3 minutes and tells you if your protein is interacting with other molecules. Since it does this in a label-free way with very little sample, it’s much easier than traditional methods, so now there’s no reason why you wouldn’t do it earlier.
Know protein quality early on
During monoclonal antibody therapeutic development, knowing structural integrity as early as possible is one of the strongest indicators of functionality and potential drug efficacy.
A monoclonal antibody (Herceptin) was treated with two oxidation conditions and run on Tycho to test the effects of the treatment on sample quality. A longer oxidation treatment caused more unfolding of the mAb as indicated by the increased initial ratio reading. In addition, increased oxidation treatment causes a left shift in the detected first inflection temperature suggesting possible structural changes to particular domains in the protein (left). MicroScale Thermophoresis (MST) was performed to confirm the effect oxidation treatment can have on Herceptin binding affinity (right).
Get Prometheus, the new gold standard for challenging stability characterizations
Prometheus has been chosen by the scientific community because it consistently delivers high-resolution data that reveals liabilities in drug candidates missed by other technologies. No other system offers simultaneous, multi-parameter characterization throughout the entire run — measuring thermal unfolding, particle sizing, and aggregation — as well as chemical denaturation for a stability profile of unmatched detail.
Prometheus consistently delivers trustworthy, high-resolution stability characterization
Get precise, high-resolution data and reliable results every time
Measuring with precision matters when there are tiny differences between your candidates. Prometheus delivers the kind of stability data you need to clearly see those differences and makes it easier to decide which candidates are best to work with moving forward.
Perform simultaneous measurements with the same samples throughout the entire run
Since you’re doing multi-parameter characterization on the same samples in the same run, you gain a deeper understanding of your molecule’s behavior when correlating your conformational and colloidal stability results.
Choose your throughput, and then choose manual or automated
Be prepared to handle any project that comes your way. Characterizing stability at different checkpoints in your workflow calls for flexible throughput — early development stages require characterizing more candidates than later, during formulation. Choose to run any number of samples from 1 to 48 or 24 at a time. Add automation and do 1536 before having to reload.
Measure label-free under native conditions
Prometheus detects intrinsic fluorescence so you don’t have to introduce dyes and risk interference. It gets better — no need for sample dilution or special buffer conditions means very little or no sample prep. And, have viscous samples? No problem.
Where Prometheus is making a difference
Drug discovery & development
Use every time stability needs to be characterized is monitored to rank molecule candidates
Maximize protein solubility and stability before crystallization to dramatically increase its probability of crystallization
Differentiate viral vectors serotypes during development and manufacturing based on their thermal stability profiles
Biologics discovery & development
Compounds screening before affinity-based single-dose screening
Pre-formulation and formulation
Production & downstream process development
Protein expression & purification
Monitor the stability of recombinant proteins during selection of expression clones and chromatographic isolation and purification
Thermal shift assays
Screen compounds during drug development for shifts in thermal unfolding to eliminate compounds that decrease stability
Monitor stability of recombinant proteins during chromatographic isolation and purification
A system for every one of your needs, present or future
It’s important to take into account your evolving needs for stability characterization and throughput. Choosing fully-featured Prometheus Panta gives you the peace of mind of knowing you’ll be ready for projects that demand simultaneous, multi-parameter characterization. If having a path to automation is what you and your stakeholders have in mind, go with the Prometheus NT.Plex.
Choose Prometheus Panta if you want everything under the sun in stability characterization, including thermal unfolding, particle sizing, chemical denaturation, and aggregation.
Your best bet when you want an easy path to automation. Get thermal unfolding and chemical denaturation with optional backreflection for aggregation evaluation.
Start here for thermal unfolding and chemical denaturation with optional backreflection for aggregation evaluation.
Automated operation for unattended stability characterization
Prometheus NT.Plex plus NT.Robotic Autosampler
The Prometheus NT.Plex is transformed into a system that increases your throughput with unattended operation with the addition of the NT.Robotic Autosampler. A stand-alone all-inclusive system — with robotic arm, enclosure, computer and monitor. Load up to four 384-well plates with 1,536 samples for hands-free characterization of thermal unfolding and chemical denaturation in a single experiment. Get the optional plate temperature control to keep your samples at 4 to 20 °C while they wait in the queue. And the aggregation detection optics is another upgrade to get you complete stability characterization.
Tackle challenging stability characterizations with multiple technologies in one instrument
Prometheus utilizes a number of technologies to characterize thermal unfolding, particle sizing, and aggregation. Each one tells a different story about their stability, and are used for a variety of applications. But they have one thing in common — they are all label-free.
When is it useful?
What does it do?
For monitoring protein purification or hit screening (thermal shift assay) during biologics formulation, developability, production, and manufacturing
It measures thermal unfolding or chemical denaturation under native conditions and label-free by detecting changes in its intrinsic fluorescence during a thermal ramp or in the presence of a chemical denaturant
When is it useful?
What does it do?
For screening recombinant proteins expressed from different constructs, biologics formulation screening, sample optimization for biophysical assays, and characterization of self-interactions
It detects molecule aggregates to determine the size of proteins over a wide concentration range
When is it useful?
What does it do?
Anytime you’re looking at aggregates larger than 12.5 nm radius
It determines aggregation status by measuring light intensity loss due to scattering
Parameters that characterize protein stability and particle sizing
Do you wonder what attributes are used the most when looking at protein stability? These are the parameters researchers look at when characterizing the propensity of proteins to unfold and aggregate in response to binding events, self-interactions, temperature changes, or the presence of certain chemicals.
See how you can characterize both thermal unfolding and chemical denaturation with nanoDSF
Cm or C50
ΔG and ΔΔG
kD and D0
See how you can select the best buffer formulation using DLS
See how a team at Boehringer Ingelheim used thermal unfolding and aggregation to predict the stability of their candidate molecules
What researchers look for when selecting an instrument to characterize stability
Characterizing a candidate molecule’s stability with an instrument that has high specificity, high sensitivity, a broad limit of detection, is very accurate as well as very precise, and produces high resolution data makes a huge difference. It allows you to identify or anticipate structural liabilities that render your molecule non-manufacturable. It also helps to minimize costly mistakes like progressing a candidate that will ultimately not make it to the clinic.
With Prometheus, never doubt the quality of your measurements and move forward with confidence knowing your decisions are derived from the highest quality data.
High level of specificity
Distinguishes the signal of your biologic from the signal of the buffer or matrix
High level of sensitivity
Identifies samples and domains with subtle signals
Broad limit of detection
Measures samples at both clinically and developmentally relevant concentrations, including both high and low concentrations
Reports true Tms
Provides reliable results that consistently return the same value with little error consistent and reliable results with small standard deviations or errors that do not vary from day-to-day
Detects multiple unfolding events discriminates domains with similar Tms
Discover how Prometheus’s specificity, sensitivity, accuracy, precision, and limit of detection made a difference in biologics stability characterization
Knowing the strength of the interactions between key players will give you the insights you need to understand the details behind how biological systems work.
If you’re having difficulty studying challenging interactions that include membrane proteins, PROTACs, intrinsically disordered proteins (IDPs), or RNA-based therapeutics, you’ll need Monolith to characterize them.
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 Kds 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 Kd 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.
Membrane proteins, intrinsically disordered proteins (IDPs), receptors, enzymes, antibodies, and nanobodies
Fragments, PROTACs, ions, nanoparticles, peptides, and carbohydrates
DNA, RNA, and aptamers
Exosomes and liposomes
Platelets and whole cells
Virus particles and empty capsids
Evaluate more than a binary interaction
Assess relative affinities of two or more molecules for the same target
Ternary binding events
Characterize interactions that involve three or more binding partners
Derive additional information from your affinity assays
Oligomerization and aggregation
Monitor these events to understand protein functionality
Calculate molecular ratios of binding partners
Derive ∆G, ∆H and ∆S from calculated Kds
*Requires offline data handling, not supported by Monolith software
Use MST technology to measure interactions
Monolith uses MST technology to quantify molecular interactions between a target and ligand by detecting changes in fluorescence intensity while a temperature gradient is applied over time (grey box, top figure). The fluorescent signal comes from the target that is either fluorescently labeled or has intrinsic fluorescence and becomes an extremely sensitive reporter for the interaction. The binding affinity is automatically determined at the end of each run without additional and lengthy data analysis. The affinity constant (Kd) is calculated from a fitted curve that plots normalized fluorescence against concentration of ligand (bottom figure).
Monolith has no fluidics — that means there’s really no regular maintenance
Life is so much easier when fluidics aren’t involved. Monolith doesn’t require cleaning or flushing in between runs, or a maintenance contract. So, it’s ready whenever you’re ready.
NanoTemper Tech has not received any reviews.
NanoTemper Tech has not received any endorsements.