| Description | PS315 inhibits the full-length and catalytic domain constructs of PKCζ (IC50=10 μM) and PKCη (IC50=30 μM). PS315 has anti-cancer activity. PS315 is a derivative of PS48 and is an allosteric PKC inhibitor by binding to the PIF-pocket of aPKC and inducing displacement of the active site residue Lys111. |
| In vitro | PS315, binding at the PIF-pocket, induces a displacement of the active site residue Lys111, thereby inhibiting the activity of aPKCs by allosterically affecting the catalytic mechanism of the kinase. Preincubation of U937 cells with 5 μM PS315 inhibits TNF-α caused NF-κB activation by 74%, whereas complete inhibition is observed with 10 μM PS315. The small allosteric inhibitor PS315 and the N-terminal region of aPKC both act directly on the PIF-pocket on-off switch[1]. |
| Target activity | PKCη:30 μM, PKCζ:10 μM |
| molecular weight | 362.85 |
| Molecular formula | C23H19ClO2 |
| CAS | 1221964-50-6 |
| Storage | Powder: -20°C for 3 years | In solvent: -80°C for 1 year |
| References | 1. Zhang H, et al. Molecular mechanism of regulation of the atypical protein kinase C by N-terminal domains and an allosteric small compound. Chem Biol. 2014 Jun 19;21(6):754-65. |