TRF2 Lentiviral Activation Particles (h): sc-401289-LAC

TERF2 encodes telomeric repeat-binding factor 2 (TRF2), a core component of the shelterin complex that binds double-stranded telomeric DNA to preserve chromosome end integrity. TRF2 suppresses aberrant ATM-dependent DNA damage signaling and classical non-homologous end joining at telomeres, thereby preventing telomere end-to-end fusions and maintaining genome stability during replication. Through coordination of telomere loop (T-loop) formation and telomere replication, TRF2 influences cell-cycle progression, replicative capacity, and senescence programs. Dysregulated TERF2/TRF2 function is implicated in telomere dysfunction, chromosomal instability, and altered DNA damage responses that are relevant to studies of cancer biology, aging, and telomere-related genome maintenance disorders.

TRF2 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 TERF2 upregulation across a broader range of human cell types.

TRF2 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 TERF2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous TRF2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native TERF2 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.