| Bioactivity | 4-Phenoxybenzylamine inhibits the function of the NS3 protein by stabilizing an inactive conformation with an IC50 of about 500 μM against FL NS3/4a. |
| Target | IC50: 500 μM (FL NS3/4a) |
| Invitro | A highly conserved novel binding site located at the interface between the protease and helicase domains of the Hepatitis C Virus (HCV) NS3 protein is identified. 4-Phenoxybenzylamine binding at this allosteric site inhibits the function of the NS3 protein by stabilizing an inactive conformation and thus represents a new class of direct acting antiviral agents[1]. |
| Name | 4-Phenoxybenzylamine |
| CAS | 107622-80-0 |
| Formula | C13H13NO |
| Molar Mass | 199.25 |
| Appearance | Liquid |
| Transport | Room temperature in continental US; may vary elsewhere. |
| Storage | 4°C, protect from light *In solvent : -80°C, 6 months; -20°C, 1 month (protect from light) |
| Reference | [1]. Saalau-Bethell SM, et al. Discovery of an allosteric mechanism for the regulation of HCV NS3 protein function. Nat Chem Biol. 2012 Nov;8(11):920-5. |
4-Phenoxybenzylamine
CAS: 107622-80-0 F: C13H13NO W: 199.25
4-Phenoxybenzylamine inhibits the function of theNS3 protein by stabilizing an inactive conformation with an IC50 of abo
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