POT1 Lentiviral Activation Particles (h): sc-403275-LAC

Human POT1 (protection of telomeres 1) encodes a core component of the shelterin complex that binds the single-stranded 3′ telomeric overhang, limiting aberrant ATR-dependent DNA damage signaling and regulating telomerase access. By coordinating telomere capping, end processing, and replication fork progression through telomeric repeats, POT1 helps preserve chromosome end integrity and genome stability. Disruption of POT1 function is linked to telomere dysfunction, altered telomere length homeostasis, and elevated chromosomal instability, processes relevant to studies of tumor predisposition and hematologic and cutaneous malignancy-associated biology. POT1 is therefore widely used as a node for interrogating DNA damage response pathways, replication stress at repetitive DNA, and mechanisms controlling telomere maintenance.

POT1 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 POT1 upregulation across a broader range of human cell types.

POT1 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 POT1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous POT1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native POT1 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.