QIP1 Lentiviral Activation Particles (h): sc-405442-LAC

KPNA4 encodes karyopherin alpha 4 (QIP1), an importin-α family adaptor that recognizes classical nuclear localization signals and partners with importin-β to mediate RanGTP-dependent nuclear import. Through control of nucleocytoplasmic trafficking, KPNA4 influences the nuclear availability of transcription factors, DNA repair proteins, and cell-cycle regulators, thereby shaping gene expression programs and stress responses. Altered importin-α–mediated transport has been linked to dysregulated proliferation, inflammatory signaling, and oncogenic phenotypes, making KPNA4 a useful node for studying nuclear transport dependencies. KPNA4/QIP1 is therefore relevant to investigations of signaling-to-transcription coupling, chromatin-associated processes, and disease-associated changes in nuclear import dynamics.

QIP1 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 KPNA4 upregulation across a broader range of human cell types.

QIP1 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 KPNA4 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous QIP1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native KPNA4 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.