P2X6 Lentiviral Activation Particles (h): sc-416264-LAC

P2RX6 encodes the P2X6 receptor, an ATP-gated cation channel of the purinergic P2X family that contributes to rapid Na⁺ and Ca²⁺ influx and downstream membrane depolarization in excitable and non-excitable cells. P2X6 can assemble as a functional subunit within heteromeric P2X receptor complexes, shaping receptor trafficking, kinetics, and ATP sensitivity. Through regulation of intracellular calcium signaling, P2X6 influences pathways linked to neurotransmission, neuroimmune communication, and stimulus-evoked inflammatory responses. Dysregulated purinergic signaling involving P2X family members has been associated with neurological and inflammatory disease mechanisms, making P2RX6 a useful target for dissecting ATP-driven signaling networks.

P2X6 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 P2RX6 upregulation across a broader range of human cell types.

P2X6 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 P2RX6 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous P2X6 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native P2RX6 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.