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Optimization of a high-throughput fluorescence polarization assay for STAT5B DNA binding domain-targeting inhibitors

J Pharm Biomed Anal. 2020; 
Pimyupa Manaswiyoungkul, Fettah Erdogan, Olasunkanmi O Olaoye, Aaron D Cabral, Elvin D de Araujo, Patrick T Gunning
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PCR Cloning and Subcloning … The corresponding mutant proteins were purified using the same procedure as the WT isoform [10,11]. All molecular cloning was performed by GenScript. The catalytic domain of ABL kinase was expressed and purified using previously described procedures [12,13] … Get A Quote

摘要

Signal transducer and activator of transcription 5B (STAT5B) is constitutively activated in multiple cancers as a result of hyperactivating mutations or dysregulation of upstream effectors. Therapeutic strategies have predominantly targeted the Src homology 2 (SH2) domain to inhibit STAT phosphorylation, a prerequisite for STAT5B transcriptional activation. An alternative approach for STAT5B pharmacologic inhibition involves targeting the DNA-binding domain (DBD). However, this strategy remains relatively unexplored and is further hindered by the lack of a high-throughput in vitro engagement assay. Herein, we present the development and optimization of a STAT5B DBD fluorescence polarization (FP) assay, which fa... More

关键词

Assay development, DNA-binding domain (DBD), Fluorescence polarization, Oligonucleotide, Signal transducer and activator of transcription (STAT), Small molecule inhibitor