Nano DSC and DSC Auto - 14 Pages

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Catalogue excerpts

Microcalorimetry Isothermal titration calorimetry (ITC) and differential scanning calorimetry (DSC) are powerful analytical techniques for in-depth characterization of molecular binding events and structural stability. Thermodynamic binding signatures not only reveal the strength of a binding event, but the specific or nonspecific driving forces involved. Structural stability profiles from DSC reveal strengths and weaknesses in higher order structure and define the behavior of individual domains and their interactions. The TA Instruments Affinity ITC, Nano ITC and Nano DSC provide the performance,...

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The Nano DSC has the versatility and precision for characterizing molecular stability, determining high affinity ligand binding and deconvoluting multi-domain structures. There is no other DSC with the proprietary technologies, high performance or the sample throughput of the Nano DSC and Nano DSC Auto. Features: • Highest sensitivity, lowest cell volume for unmatched performance • Capillary cell design for analysis of samples that tend to aggregate or precipitate • Built-in precision pressurizing system maintains accurate, constant pressure in the cells • Solid-state thermoelectric elements for...

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The Nano DSC is designed for ultra-sensitive measure of heat absorbed or released by dilute in-solution bio-molecules as they are heated or cooled. The capillary cell design, solidstate thermoelectric temperature control and easy cleaning ensure the highest sensitivity and data reproducibility for a wide variety of applications. Features: • 300 µL active volume capillary cells for analyzing hydrophobic samples • Easy, accurate sample loading with laboratory pipetteman • Built-in, user-programmable pressurization system (up to 6 atm) • Flexible data acquisition interface for easy experiment setup...

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Pressure Ring The NanoDSC is a powerful thermal scanning instrument that utilizes a 300 µL capillary cell design and solid-state thermoelectric temperature control to provide unmatched performance. Nano DSC Capillary Platinum Cells Thermoelectric Device • Fixed-in-place capillary cells attenuate aggregation and precipitation • Platinum cells are inert and compatible with strong acids, bases and protein cleaning enzymes • 300 µL active cell volume minimizes sample consumption • Sample cell loading with laboratory pipetteman is easy and ensures no trapped air bubbles Nano DSC Solid-State Thermoelectric...

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The Nano DSC Autosampler enables true “start and walk away” capability without sacrificing either sensitivity or reliability. It is an industry-proven 96-well plate autosampler that stores and delivers samples to the DSC cells. User-programmable washing routines ensure no sample carry over and the 96-well format maximizes sample throughput. Autosampler Features: • Industry-proven HPLC autosampler reliability • Easy connection to the Nano DSC through autosampler interface • Two (2) 96-well plates store samples at temperatures down to 4°C • Four (4) wash/rinse solvent ports on the autosampler interface...

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Molar Heat Capacity How much Protein is Required for a DSC Scan? Determining the thermodynamic parameters of a protein by differential scanning calorimetry (DSC) using the Nano DSC requires about the same amount of protein as surface plasmon resonance or fluorescence studies. Because of the Nano DSC’s extreme sensitivity and baseline reproducibility, and the sample cell’s small volume (300 µL), a complete, interpretable, accurate scan can be obtained on essentially any protein of interest. The sensitivity and accuracy of the Nano DSC is demonstrated by this data. Hen egg white lysozyme (in pH...

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Analyzing the stability of a protein in dilute solution involves determining changes in the partial molar heat capacity of the protein at constant pressure (∆Cp). The contribution of the protein to the calorimetrically measured heat capacity (its partial Cp) is determined Heat Flow/µW Characterization of Protein Stability by subtracting a scan of a buffer blank from the sample data prior to analysis. Heating the protein sample initially produces a slightly increasing baseline but as heating progresses, baseline scans heat is absorbed by the protein and causes it to thermally unfold over a temperature range...

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Investigation of Protein-Ligand Binding DSC is a valuable tool for studying binding between a biological macromolecule and a ligand such as another biopolymer or a drug. Unlike ITC, DSC allows the thermodynamics that drive binding to be correlated with conformational changes in the macromolecule caused by the binding reaction. DSC is particularly useful for characterizing very tight or slow binding interactions. DSC also allows characterization of binding reactions that are incompatible with the organic solvent requirements of some ITC experiments (i.e., where ligand solubility for an ITC experiment...

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Instrument Control & Data Acquisition Software The Affinity and Nano instruments control and data acquisition functions are executed within a Windows-compatible software interface, ITCRun or DSCRun. All experimental parameters and sample information are easily entered into an intuitive graphical user interface and can be saved as an experimental template for future use. Real-time monitoring of the raw data as the experiment progresses allows rapid assessment of the data quality and instrument performance in individual tabs. Unique icon-controlled functions, such as immediate baseline subtraction,...

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All ITC and DSC raw data files are easily and quickly analyzed with a powerful ITC/DSC data analysis software, NanoAnalyze. Individual window tabs for each processing step guide the user through the analysis of Individual raw data files or the batch processing of multiple files. NanoAnalyze™ features: • Easy import of all ITC and DSC raw data files • User selectable fitting models for ITC and DSC Corrected Heat Rate (µJ/s) Data Analysis with NanoAnalyze™ • Easy set up of new fitting models • Powerful experiment design and optimization tool quality images All instrument control, data acquisition...

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