The levels of protein and RNA were verified by Western and Northern blots, respectively. In brief, cultured cells were harvested with trypsinization and lysed by RIPA lysis buffer (25 mM Tris–HCl pH7.6, 150 mM NaCl, 1% NP-40, 1% Sodium deoxycholate, 0.1% SDS) for total protein extraction. Each Western sample contains 30 ug total protein that was denatured in loading buffer (50 mM Tris·HCl, pH 6.8, 2% SDS, 6% Glycerol, 2 mM DTT, 0.01% Bromophenol Blue) by heated at 95 °C for 5 min, followed by separation with denature protein electrophoresis (SDS-PAGE). Separated protein samples were transferred to PVDF membrane, followed by staining with specific primary (anti-c-myc, anti-beta-actin, anti-Fluc, anti-Rluc, anti-EGFP, etc.) and HRP-conjugated secondary (anti-rabbit or anti-mouse) antibodies. RNA samples were prepared following the protocol described by Mordstein et al. (2020 (link)) with TRIzol™ Reagent (Invitrogen, USA). Cytosolic fractions of RNAs were separated with denature agarose electrophoresis, followed by transferring to nylon blotting membranes. Transferred membrane were probed with digoxigenin (DIG) labelled Fluc- or Rluc-specific probes and then documented by chemiluminescence imager.