Transcription factors (TFs) play a crucial role in regulating gene expression and controlling a wide range of biological processes. Despite their significance, targeting transcription factors in drug discovery has traditionally been challenging. These proteins typically lack well-defined binding pockets, making it difficult to design small molecules that can modulate their activity effectively. Additionally, the complex interactions between transcription factors and DNA, as well as their involvement in multiprotein complexes, add layers of difficulty to developing targeted therapies. However, recent advancements in screening technologies, and computational modeling have revitalized interest in this field, opening new avenues for therapeutic interventions.
At ICE Bioscience, we specialize in addressing challenging drug targets that were once considered undruggable and have developed a comprehensive suite of assays to evaluate the potency and efficacy of compounds across various transcription factors. These factors influence human tumor suppression, the inflammatory stress response, and essential cellular processes necessary for homeostasis.
✅ Biophysical and Biochemical Assays:
Surface Plasmon Resonance (SPR): Used for real-time binding analysis of transcription factors such as STAT proteins (e.g., STAT1, STAT2) and complexes like c-Myc, providing interaction data with compounds.
Fluorescence Polarization (FP): Applied in assays for nuclear receptors (e.g., AR), detecting binding interactions with compounds such as DHT and Enzalutamide.
TR-FRET and AlphaLISA: These technologies are used for detecting binding interactions across various targets, including STAT family proteins, IRF5, and the c-Myc/Max/DNA complex.
✅ Cell-Based Assays:
Reporter Gene Assays: Employed to assess transcription factor activity in live cells by monitoring gene expression changes, providing a direct readout of transcription factor regulation.
Phosphorylated STAT Detection: ELISA, flow cytometry, and similar methods are available to quantify levels of phosphorylated proteins (e.g., pSTAT), which are indicators of transcription factor pathway activation.
Note: p53 assays are covered separately here.
| Target | Assay Type | Reference Compound | Assay Format |
|---|---|---|---|
| STAT1 | Binding | SI-109 | SPR |
| STAT2 | Binding | SI-109 | SPR |
| STAT3 | Binding | SI-109 | TR-FRET |
| STAT3 | Binding | SI-109 | SPR |
| STAT4 | Binding | SI-109 | TR-FRET |
| STAT4 | Binding | SI-109 | SPR |
| STAT5A | Binding | SI-109 | SPR |
| STAT5B | Binding | SI-109 | TR-FRET |
| STAT5B | Binding | SI-109 | SPR |
| STAT6 | Binding | SI-109, STAT6-IN-3 | TR-FRET |
| STAT6 | Binding | SI-109 | SPR |
| AR | Binding | DHT, Estradiol, Enzalutamide | FP |
| GR | Binding | Mifepristone, Mometasone furoate | TR-FRET |
| Nrf2 | Binding | KI696 | TR-FRET |
| c-Myc | Binding | MYCi361 | SPR |
| c-myc/max | Binding | 3jc48-3 | AlphaLISA |
| c-myc/max/DNA | Binding | 3jc48-3 | AlphaLISA |
| c-myc&WDR5 | Binding | c-myc peptide | TR-FRET |
| IRF5 | Binding | CPP5 | TR-FRET |
| IRF5 | Binding | YE6144, N5-1 | SPR |
| avi-IRF5 S430D | Binding | YE6144, N5-1 | SPR |
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