"Part of our research focus on the protein structural-function basis for iron metabolism of pathogenic microorganisms. We measured the dissociated constant for periplasmic binding protein and siderophore through MST technology. Because siderophore is extremely insoluble, it's difficult for us to complete that task via other methods such as ITC and SPR. We strongly recommend MST technology for its low material consumption, short measurement time and very wide application range."

"Our recent research is focused on the critical pathogenic protein & complex from pathogenic microbes and the Protein structure-functional basis for some endogenous disease. Via MST, we measured the Protein-DNA interaction, that have been difficult to detect and quantify with other standard biomolecule interaction technologies (like SPR and ITC) because of the conformation/immobilization-sensitive and very little heat changes of our samples. MST technology can be used as a complementary technology to the traditional methods in these fields. We can strongly recommend MST technology for its low material consumption, short measurement times and broad application range for molecule-interaction studies."

"Our recent research is focused on the molecular basis of herbicide resistance and exploiting new target sites of herbicide, such as PPI of AHAS. Via MST, we measured the Protein-Protein interaction, that have been difficult to detect and quantify with ITC because of instability of the protein and very little heat changes of our samples. The MST technology can be used as a complementary technology to the traditional methods in these fields. We can strongly recommend the MST technology for its low material consumption, short measurement times and broad application range in the field of molecule interaction studies."

"We are interested in applying computational fragment-based strategy to identify lead compounds to block protein-protein interactions in RAS pathway. Generally, the identified fragments are weak binders with binding affinities ranging from millimolar to micromolar. For such weak interactions, it is difficult to set up reliable biochemical assays or binding assays using ITC or SPR techniques. Fortunately, MST technology turns out to be an excellent way to determine such weak interactions between small fragments and protein in our system of interest. We efficiently and reliably performed our experimental binding measurement using minimum amount of protein and fragments.

We are also interested in studying the regulation mechanism of a nuclear hormone receptor, which plays fundamental role in homeostasis and metabolism. The nuclear hormone receptor can be modified by an important enzyme to regulate the expression of specific genes and cause certain metabolic disease. We wanted to measure the binding affinity between these two proteins. Interestingly, this interaction is extremely difficult for the standard binding affinity measurement approach, with no exothermal or endothermal signals using ITC. While using MST technology, we have successfully detected this interaction. We strongly recommend MST technology for its low material consumption, short measurement time, and very high sensitivity."

We used Microscale Thermophoresis (MST) to measure the interaction between large molecular chaperones with molecular weight up to 800 kDa. It is distinguished in low sample consumption, fast measurement and immobilization-free setup. We found that the biophysical data obtained from MST are in good agreement with those obtained from SPR or ITC. MST technology will facilitate our research on various interactions.

Our lab focuses on the importance for telomere and telomerase to maintain the integrity of genomes and the stability of chromosomes. Large amount of proteins and protein complexes are involved in epigenetics, which play essential rotes in controlling many cellular events. We are employing MicroScale Thermophoresis (MST) in determining the interactions of proteins/protein complexes to ssDNA/RNA. It's easier to measure the protein-protein or protein-nucleic acid interaction, especially for those sensitive samples, that has been difficult to detect and quantify with ITC or SPR. We benefited from the low sarnple consumption, the fast measurements, the broad application range and the possibility to choose the buffer freely, resulting in highly reproducible data. We strongly recommend MST technology for its low material consumption, short measurement times and very high sensitivity.