VRL-1 Lentiviral Activation Particles (h): sc-401648-LAC

TRPV2 encodes the vanilloid receptor-like 1 (VRL-1), a Ca²⁺-permeable nonselective cation channel of the TRP superfamily that responds to mechanical stress, heat, and lipid mediators. VRL-1–dependent calcium influx regulates membrane excitability, cytoskeletal remodeling, and vesicular trafficking, linking channel activity to Ca²⁺/calmodulin signaling, MAPK responses, and downstream transcriptional programs. In immune and myeloid lineages, TRPV2 has been implicated in chemotaxis and phagocytic function, while in excitable and stromal contexts it can influence cellular migration and differentiation states. Dysregulated TRPV2 signaling has been studied in models of inflammation, neuropathic pain–related pathways, cardiomyocyte stress responses, and tumor-associated phenotypes, supporting its value as a mechanistic target in pathway-focused research.

VRL-1 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 TRPV2 upregulation across a broader range of human cell types.

VRL-1 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 TRPV2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous VRL-1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native TRPV2 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.