Thermal Shift Assay (TSA) is a versatile and reliable technique for assessing protein stability under various conditions. Using extrinsic fluorescent dyes, TSA monitors the thermal unfolding of proteins by detecting fluorescence changes as the protein denatures. This method provides critical insights into protein-ligand interactions, buffer optimization, and formulation development. With its high sensitivity and compatibility with widely available instruments, TSA is an ideal solution for studying protein stability, identifying stabilizing conditions, and supporting drug discovery workflows.
Principles of TSA assay. Proteins typically exist in their native, folded state. As the temperature increases, the thermal motion of the protein molecules intensifies, leading to unfolding and the exposure of hydrophobic regions. During this process, a fluorescent dye binds to these newly exposed hydrophobic regions, causing an increase in fluorescence intensity. Once the temperature reaches a critical point (the melting temperature, Tm), the unfolded proteins aggregate, preventing further dye binding. This results in the dye returning to the aqueous environment, causing fluorescence quenching. Consequently, the fluorescence intensity initially increases and then decreases, forming a characteristic "melting curve." By plotting fluorescence intensity against temperature, the Tm of the protein can be determined.
High Sensitivity and Accuracy: Leveraging the advanced QuantStudio 7 Flex system, our TSA service provides precise detection of protein melting temperatures (Tm) for reliable stability assessments.
Versatile Applications: Supports buffer optimization, ligand screening, and formulation studies, offering a comprehensive solution for protein stability and drug discovery workflows.
High Throughput: Compatible with 96- and 384-well plates, enabling the analysis of multiple samples or conditions efficiently and cost-effectively.
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