PRMT5 Lentiviral Activation Particles (h): sc-401115-LAC

PRMT5 encodes protein arginine methyltransferase 5, a major type II methyltransferase that catalyzes symmetric dimethylation of arginine residues on histones and numerous non-histone substrates. Through regulation of chromatin accessibility, transcriptional programs, and RNA splicing, PRMT5 influences core processes including cell-cycle progression, DNA damage responses, ribosome biogenesis, and stemness-associated gene expression. PRMT5 activity interfaces with epigenetic and signaling networks such as MYC-driven transcription, p53 pathway modulation, and spliceosomal assembly via Sm protein methylation. Dysregulated PRMT5 expression or function has been associated with altered proliferation, lineage specification, and oncogenic transformation across multiple tumor contexts, supporting its use as a mechanistic node for studying epigenetic control of disease-relevant phenotypes.

PRMT5 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 PRMT5 upregulation across a broader range of human cell types.

PRMT5 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 PRMT5 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous PRMT5 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native PRMT5 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.