USP47 Lentiviral Activation Particles (h): sc-403157-LAC

USP47 (ubiquitin specific peptidase 47) is a human deubiquitinating enzyme that removes ubiquitin from protein substrates to modulate their stability, localization, and signaling output. By editing ubiquitin-dependent protein turnover, USP47 contributes to proteostasis and influences pathways linked to DNA damage signaling, cell-cycle control, and stress responses through regulation of ubiquitination dynamics. Altered deubiquitination networks involving USP47 have been associated with dysregulated growth and genome maintenance programs observed in multiple disease contexts, supporting its investigation as a node in ubiquitin–proteasome and repair-associated circuitry. Functional studies commonly assess how USP47-dependent deubiquitination reshapes transcriptional programs and pathway activity under basal conditions or after genotoxic challenge.

USP47 Lentiviral Activation Particles (h) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient USP47 upregulation across a broader range of human cell types.

USP47 Lentiviral Activation Particles (h) deliver all functional components of the synergistic activation mediator (SAM) system via lentiviral transduction. The system comprises three particle preparations co-transduced into target cells: one encoding catalytically inactive dCas9 (D10A and N863A mutations) fused to the VP64 transactivation domain with a blasticidin resistance gene; one encoding the MS2-p65-HSF1 fusion protein with a hygromycin resistance gene; and one encoding a target-specific 20 nt sgRNA fused to two MS2 RNA aptamers with a puromycin resistance gene. Following lentiviral transduction and genomic integration of the expression cassettes, the SAM components are stably expressed and assemble at the target locus within the proximal promoter region upstream of the USP47 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous USP47 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native USP47 genomic locus and regulatory architecture.

The lentiviral format offers several practical advantages: stable genomic integration supports heritable activation across cell divisions; high-titer particle preparations eliminate the need for in-house viral production; and compatibility with primary, non-dividing, and transfection-resistant cell types expands experimental accessibility. Successful transduction can be confirmed and enriched through triple antibiotic selection using puromycin, hygromycin, and blasticidin.

For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.