Affinity. Stability. Conformation.
NanoTemper Technologies, headquartered in Munich, Germany, is a leading provider of highly innovative instrumentation and software solutions for biomolecular analytics. We are driven by the unique demands of science and committed to developing high-quality instruments that push the limits of speed, efficiency and precision. Our proprietary technologies are used by pharmaceutical and basic research scientists across four continents. We back our products with unparalleled customer care through a team of experts at our global application support centers. NanoTemper Technologies has received the German Innovation Award (2012), the Bavarian Export Prize (2013) and the Deutscher Gründerpreis (German Founders Award; 2014).
Monolith: More than binding affinities
The Monolith NT.115 uses MicroScale Thermophoresis (MST) to quantify biomolecular interactions and calculate dissociation constants (Kd) in an easy, rapid and accurate way. During an MST experiment, molecules move along a microscopic laser-induced temperature gradient. Upon binding, the molecule of interest changes its migration behavior, which is detected using covalent dyes, fluorescent fusion proteins or intrinsic fluorescence (Monolith NT.LabelFree). By combining the precision of fluorescence detection with the flexibility and sensitivity of thermophoresis, Monolith instruments provide a flexible, robust and highly versatile platform for measuring molecular interactions. The fully-automated Monolith NT.Automated is designed for easy handling and high-throughput applications. The instrument can be integrated in a liquid handling platform to allow several hours of unsupervised data acquisition. The capillary chips are easy to use and avoid any equilibration or washing downtime. Thus, the Monolith NT.Automated is ideal for screening and hit identification applications.
Prometheus: Rapid & easy protein stability analysis
Prometheus NT.48 is based on nanoDSF, an advanced Differential Scanning Fluorimetry technology that uses intrinsic tryptophan and tyrosine fluorescence to measure protein folding and stability in a label-free manner. The capillary format eliminates instrument maintenance requirements and enables precise measurements and easy sample handling, even for highly viscous formulation conditions or detergent-solubilized membrane proteins. The instrument provides unmatched scanning speed and data point density, revealing even small unfolding events. Prometheus instruments utilize an inverse light scattering technology to combine thermal stability analysis with determination of aggregation onset temperatures. Together with the NT.Robotic Autosampler, the Prometheus NT.Plex can be fully automated. This setup allows for unattended sample preparation, handling and measurement, and is amenable to virtually an unlimited number of samples.
- Pharmaceutical Manufacturing
- Drug Development
- Pharmaceutical Laboratory Equipment
- Pharmaceutical Research
- Laboratory Instruments
- Laboratory Software
Use of iFormulate™ and nanoDSF for Fast and Precise Protein Formulation Development
One of the challenges in protein formulation is the simultaneous evaluation of multiple key formulation variab...
Site-Specific Labeling of Antibodies for MicroScale Thermophoresis
Site-specific conjugation of a dye to antibodies is useful for producing highly homogeneous material for use i...
Protein-Protein Interaction Analysis in Different Buffer Systems
Using MST to analyse the binding of the β-Lactamase TEM1 to BLIP
Protein-Ion Interaction Analysis
Binding of Calcium Ions to Synaptotagmin measured with fluorescence label and label-free
Studying the interaction of membrane enzyme PgIB with substrate and inhibitory peptide
Studying the interaction of the antibody-drug conjugate SYD985 with an anti-toxin antibody
One-step, purification-free and site-specific labeling of polyhistidine-tagged proteins for MST
Protein Quality Control
Rapid Quantification of Unfolded Proteins for Quality Control and Optimization of Storage Conditions
Unfolding and Aggregation of mAbs
Analysis of formulation-dependent colloidal and conformational stability of monoclonal antibodies
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