EHT-5372

For research use only, not for therapeutic use.

  • CAT Number: I006632
  • CAS Number: 1425945-63-6
  • Molecular Formula: C17H11Cl2N5OS
  • Molecular Weight: 404.27
  • Purity: ≥95%
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EHT-5372(Cat No.:I006632)is a potent and selective small-molecule inhibitor of fibroblast growth factor receptor 4 (FGFR4). This compound plays a key role in modulating FGFR4 activity, making it valuable for cancer research, particularly in studies focusing on liver cancer and other FGFR4-driven tumors. Its specificity allows for the investigation of FGFR4’s function without significantly affecting other fibroblast growth factor receptors. EHT-5372’s potential in targeted cancer therapy research highlights its importance in advancing personalized medicine and understanding FGFR4-related signaling pathways.


Catalog Number I006632
CAS Number 1425945-63-6
Synonyms

EHT-5372; EHT 5372; EHT5372.;methyl 9-((2,4-dichlorophenyl)amino)thiazolo[5,4-f]quinazoline-2-carbimidate

Molecular Formula C17H11Cl2N5OS
Purity ≥95%
Target DYRK1A inhibitor
Solubility Soluble in DMSO
Storage 0 - 4°C for short term or -20 °C for long term
IUPAC Name methyl 9-(2,4-dichloroanilino)-[1,3]thiazolo[5,4-f]quinazoline-2-carboximidate
InChI InChI=1S/C17H11Cl2N5OS/c1-25-15(20)17-24-12-5-4-11-13(14(12)26-17)16(22-7-21-11)23-10-3-2-8(18)6-9(10)19/h2-7,20H,1H3,(H,21,22,23)
InChIKey QSGKPYRFWJINEH-UHFFFAOYSA-N
SMILES COC(=N)C1=NC2=C(S1)C3=C(C=C2)N=CN=C3NC4=C(C=C(C=C4)Cl)Cl
Reference

1:J Med Chem. 2016 Nov 23;59(22):10315-10321. Epub 2016 Nov 2. An Unusual Binding Model of the Methyl 9-Anilinothiazolo[5,4-f] quinazoline-2-carbimidates (EHT 1610 and EHT 5372) Confers High Selectivity for Dual-Specificity Tyrosine Phosphorylation-Regulated Kinases.Chaikuad A,Diharce J,Schröder M,Foucourt A,Leblond B,Casagrande AS,Désiré L,Bonnet P,Knapp S,Besson T, PMID: 27766861 DOI: 10.1021/acs.jmedchem.6b01083 </br><span>Abstract:</span> Methyl 9-anilinothiazolo[5,4-f]quinazoline-2-carbimidates 1 (EHT 5372) and 2 (EHT 1610) are strong inhibitors of DYRK/’s family kinases. The crystal structures of the complex revealed a noncanonical binding mode of compounds 1 and 2 in DYRK2, explaining the remarkable selectivity and potency of these inhibitors. The structural data and comparison presented here provide therefore a template for further improvement of this inhibitor class and for the development of novel inhibitors selectively targeting DYRK kinases.

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