IFT88 Lentiviral Activation Particles (h): sc-404089-LAC

Human IFT88 encodes a core component of the intraflagellar transport B (IFT-B) complex that drives anterograde trafficking along the primary cilium, enabling assembly and maintenance of the axoneme and proper ciliary signaling. By supporting cilium-dependent signal transduction, IFT88 influences pathways such as Hedgehog and other sensory receptor–coupled processes that depend on intact ciliary structure and protein movement. Disruption or dysregulation of IFT88 perturbs ciliogenesis, alters downstream transcriptional programs, and impacts cell-cycle and polarity control in ciliated cell types. Consequently, IFT88 is widely studied in the context of ciliopathies, renal and retinal phenotypes, and developmental signaling defects where primary cilium function is a central variable.

IFT88 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 IFT88 upregulation across a broader range of human cell types.

IFT88 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 IFT88 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous IFT88 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native IFT88 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.