PSMD1 Lentiviral Activation Particles (h): sc-405171-LAC

PSMD1 encodes a core non-ATPase subunit of the 19S regulatory particle of the 26S proteasome, supporting ubiquitin-dependent recognition, deubiquitination-coupled processing, and delivery of substrates to the 20S catalytic core. Through its role in the ubiquitin–proteasome system, PSMD1 influences protein homeostasis, cell-cycle progression, DNA damage responses, antigen processing, and regulation of transcription factors such as NF-κB. Perturbation of proteasome regulatory subunits can shift proteostasis networks and stress signaling, impacting pathways linked to apoptosis, inflammation, and metabolic adaptation. Altered proteasome function and expression patterns are frequently studied in contexts of cancer biology, neurodegeneration, and immune dysregulation where proteotoxic stress and protein turnover are central experimental variables.

PSMD1 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 PSMD1 upregulation across a broader range of human cell types.

PSMD1 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 PSMD1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous PSMD1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native PSMD1 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.