20S Proteasome α7 Lentiviral Activation Particles (h): sc-401897-LAC

PSMA7 encodes the 20S proteasome α7 subunit, an essential structural component of the 20S core particle that contributes to proteasome assembly and formation of the gated entry channel controlling substrate access. Through the ubiquitin–proteasome system, α7 supports ATP-dependent protein turnover that regulates cell-cycle progression, signal transduction, antigen processing for MHC class I presentation, and proteostasis under oxidative or proteotoxic stress. Perturbations in proteasome composition or activity can remodel degradation of key regulatory proteins and influence pathways such as NF-κB signaling, DNA damage responses, and apoptosis. Altered proteasome homeostasis, including changes in PSMA7 expression, has been reported across multiple disease-relevant contexts where proteostasis and immune surveillance are dysregulated, supporting its use as a mechanistic node in proteasome biology studies.

20S Proteasome α7 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 PSMA7 upregulation across a broader range of human cell types.

20S Proteasome α7 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 PSMA7 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous 20S Proteasome α7 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native PSMA7 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.