Not CRISPR data: the image illustrates antibody quality for visualizing CRISPR experiment results.
Not CRISPR data: the image illustrates antibody quality for visualizing CRISPR experiment results.
P2X7 Lentiviral Activation Particles (h2): sc-400780-LAC-2
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- P2X7 Lentiviral Activation Particles (h2) is a synergistic activation mediator (SAM) transcription activation system designed to specifically and efficiently upregulate gene expression via lentiviral transduction of cells
- P2X7 Lentiviral Activation Particles (h2) contain the following SAM Activation elements: a deactivated Cas9 (dCas9) nuclease (D10A and N863A) fused to the transactivation domain VP64, an MS2-p65-HSF1 fusion protein and a target-specific 20 nt guide RNA. They also contain the blasticidin, hygromycin and puromycin resistance genes
- Upon transduction, the SAM complex binds to a site-specific region approximately 200-250 nt upstream of the transcriptional start site and provides robust recruitment of transcription factors for highly efficient gene activation
- gRNAs encoded by P2X7 Lentiviral Activation Plasmid (h2) and P2X7 Lentiviral Activation Plasmid (h22) target distinct regulatory regions of the P2RX7 promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: P2X7 Antibody (D-1): sc-514962
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
P2X7 Lentiviral Activation Particles (h2) | sc-400780-LAC-2 | 200 µl | $455.00 |
Human P2RX7 encodes the P2X7 purinergic receptor, an ATP-gated cation channel that drives Na⁺/Ca²⁺ influx and K⁺ efflux to regulate membrane depolarization, cytokine maturation, and, under sustained stimulation, large-pore formation linked to cell death programs. P2X7 is a key modulator of innate immune signaling, coupling extracellular ATP sensing to inflammasome activation (including NLRP3), caspase-1–dependent IL-1β/IL-18 processing, and downstream NF-κB and MAPK pathway responses in myeloid cells, microglia, and other immune-relevant populations. Dysregulated P2RX7 activity and expression have been associated with chronic inflammation and neuroinflammatory processes, as well as altered immune cell function in cancer and autoimmune contexts. Gene editing of P2RX7 supports mechanistic studies of purinergic signaling, inflammatory mediator release, immune cell phenotype regulation, and stimulus-dependent cytotoxicity in physiologically relevant cellular models.
P2X7 Lentiviral Activation Particles (h2) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient P2RX7 upregulation across a broader range of human cell types.
P2X7 Lentiviral Activation Particles (h2) 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 P2RX7 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous P2X7 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native P2RX7 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.