P2X1 CRISPR Activation Plasmid (h): sc-404030-ACT
- Target species: human
- 20 µg of transfection-ready, purified plasmid DNA; Suitable for up to 20 transfections
- P2X1 CRISPR Activation Plasmid (h) is a synergistic activation mediator (SAM) transcription activation system designed to specifically upregulate gene expression
- P2X1 CRISPR Activation Plasmid (h) consists of three plasmids at a 1:1:1 mass ratio: a plasmid encoding the deactivated Cas9 (dCas9) nuclease (D10A and N863A) fused to the transactivation domain VP64, and a blasticidin resistance gene; a plasmid encoding the MS2-p65-HSF1 fusion protein, and a hygromycin resistance gene; a plasmid encoding a target-specific 20 nt guide RNA fused to two MS2 RNA aptamers, and a puromycin resistance gene
- The resulting 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 P2X1 CRISPR Activation Plasmid (h) and P2X1 CRISPR Activation Plasmid (h2) target distinct regulatory regions upstream of the P2RX1 transcriptional start site. One or both designs may be available
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
P2X1 CRISPR Activation Plasmid (h) | sc-404030-ACT | 20 µg | $397.00 |
Human P2RX1 encodes the ATP-gated cation channel P2X1, a trimeric purinergic receptor that rapidly opens in response to extracellular ATP to mediate Na+ and Ca2+ influx and membrane depolarization. P2X1 signaling contributes to purinergic neurotransmission, platelet activation, leukocyte chemotaxis, and smooth muscle contraction, linking extracellular nucleotide release to intracellular calcium-dependent pathways. Through regulation of calcium dynamics and excitability, P2X1 impacts vascular tone, thrombo-inflammatory responses, and immune cell activation programs. Altered P2RX1/P2X1 activity has been investigated in contexts including platelet function and thrombosis biology, inflammatory signaling, and reproductive tract physiology, making it a useful node for mechanistic studies of purinergic pathways.
P2X1 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous P2RX1 expression without altering the underlying DNA sequence.
P2X1 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the P2RX1 locus in human cell lines. The system is built around a catalytically inactive Cas9 (dCas9) carrying two inactivating mutations (D10A and N863A) that eliminate nuclease activity while preserving DNA binding. This dCas9 is fused to VP64, a potent transcriptional activator, and is co-expressed with a blasticidin resistance gene for selection. The second plasmid encodes the MS2-p65-HSF1 fusion protein, a secondary activator complex that works in concert with dCas9-VP64, alongside a hygromycin resistance gene. The third plasmid encodes a target-specific 20 nt sgRNA fused to two MS2 RNA aptamers that recruit the MS2-p65-HSF1 complex to the activation site, accompanied by a puromycin resistance gene. The three plasmids are delivered at a 1:1:1 mass ratio for balanced expression of all system components.
Once assembled at the target locus, the SAM complex binds within approximately 200 bp upstream of the P2RX1 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous P2X1 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native P2RX1 locus and enabling the study of P2X1-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of P2X1 pathway restoration in tumor cells with silenced or reduced P2RX1 expression.
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.