SQSTM1/p62 Lentiviral Activation Particles (h): sc-400099-LAC

Human SQSTM1 encodes sequestosome 1 (SQSTM1/p62), a multifunctional autophagy receptor and signaling scaffold that links ubiquitinated cargo to LC3-positive autophagosomes via its UBA and LIR motifs. SQSTM1/p62 coordinates selective autophagy, proteostasis, and stress responses, and modulates key pathways including KEAP1–NRF2 antioxidant signaling, NF-κB activation, and mTORC1 regulation at the lysosome. Through its role in protein aggregate clearance and innate immune signaling, altered SQSTM1/p62 activity is frequently studied in contexts of neurodegeneration, cancer biology, and inflammatory disease mechanisms. SQSTM1/p62 also contributes to organelle quality control and signaling at the crossroads of ubiquitin-dependent degradation and transcriptional programs.

SQSTM1/p62 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 SQSTM1 upregulation across a broader range of human cell types.

SQSTM1/p62 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 SQSTM1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous SQSTM1/p62 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native SQSTM1 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.