To examine whether KLF4's binding activity to M197 (CCmCpGCC) is important for transcription regulation, we employed cell-based luciferase assays using both wild-type (WT) and mutated KLF4 expression constructs.
Nonetheless, we note that both the EHMT2 and PRC2 biochemical potency is comparable to the inhibitory concentrations employed in our cell-based assays.
In the absence of selective and stress-independent small-molecule HSF1 activators, current approaches have either employed HSF1 overexpression or cell-based assays using heat shock promoter reporter constructs to explore the therapeutic potential for HSF1 activation in ameliorating pathologic imbalances in cytosolic proteostasis.
We therefore strongly recommend the use of cell-based assays when testing for masked LPS.
Recent studies employing novel flow cytometric and cell-based assays have helped to redefine hematopoiesis, and suggest that erythroid progenitors may arise from different levels of the hematopoietic tree.
To confirm that high-affinity binding to S1P also translates into inhibition, the activity of Spiegelmer® NOX-S93 was tested in two cell-based assays employing two different cell lines expressing the human receptors S1PR1 and S1PR3.
In cell-based assays employing intermolecular FRET interaction, the fluorophore pairs are typically conjugated to soluble ligands, e.g., EGF, transferrin and others, that can come into nanometer-range FRET proximity upon binding to their dimerized/oligomerized respective receptors.
Recently, cell-based assays employing fast-growing auxotrophic bacteria supplemented with bioluminescent or fluorescent reporter genes have been shown to rapidly, conveniently, and simultaneously detect multiple target molecules relevant to human diseases.
As seen in Table 1, there are differences between the two cell-based assays employed, including the reporter, cell lineage (monoclonal vs. polyclonal), number of ARE sequences located in the enhancer regions and their orientation, and basal promoter.
Cell-free and cell-based assays were employed to evaluate the antioxidant capacity.
We use structural, biochemical methods and cell-based assays to understand how cPCDHs form supramolecular inter-cellular signaling assemblies.
