CHTOP Lentiviral Activation Particles (h): sc-411874-LAC

CHTOP (chromatin target of PRMT1) is a nuclear RNA-binding protein that coordinates transcription-coupled mRNA processing by linking chromatin-associated events to pre-mRNA splicing, 3′ end formation, and mRNA export. It functions within the TREX/THO messenger ribonucleoprotein export machinery and participates in epigenetic and post-transcriptional regulation, including arginine methylation–dependent interactions that influence R-loop homeostasis and genome stability. Through these roles, CHTOP helps shape gene expression programs controlling cell-cycle progression, DNA damage responses, and differentiation. Dysregulated CHTOP expression or function has been associated with altered RNA metabolism signatures observed in cancer and other proliferative or stress-adaptive states, supporting its relevance in mechanistic studies of RNA processing–driven disease phenotypes.

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

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