PiT1 Lentiviral Activation Particles (m): sc-422988-LAC
- Target species: mouse
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- PiT1 Lentiviral Activation Particles (m) is a synergistic activation mediator (SAM) transcription activation system designed to specifically and efficiently upregulate gene expression via lentiviral transduction of cells
- PiT1 Lentiviral Activation Particles (m) 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 PiT1 Lentiviral Activation Plasmid (m) and PiT1 Lentiviral Activation Plasmid (m2) target distinct regulatory regions of the Slc20a1 promoter. One or both designs may be available
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
PiT1 Lentiviral Activation Particles (m) | sc-422988-LAC | 200 µl | $455.00 |
Mouse Slc20a1 encodes PiT1 (SLC20A1), a sodium-dependent inorganic phosphate (Pi) symporter that supports cellular phosphate uptake required for nucleotide biosynthesis, membrane phospholipid turnover, and bioenergetic homeostasis. PiT1 contributes to phosphate-sensing and nutrient-responsive signaling, intersecting with metabolic and cell-cycle control programs that influence proliferation and survival. In development and adult tissue maintenance, PiT1 activity is linked to differentiation states and extracellular phosphate availability, processes relevant to studies of mineral ion handling, tissue remodeling, and metabolic stress. Altered phosphate transport and PiT1-associated pathways have been investigated in contexts such as skeletal and vascular calcification biology, tumor cell metabolism, and inflammatory microenvironments, supporting mechanistic research into phosphate-dependent phenotypes.
PiT1 Lentiviral Activation Particles (m) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient Slc20a1 upregulation across a broader range of human cell types.
PiT1 Lentiviral Activation Particles (m) 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 Slc20a1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous PiT1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Slc20a1 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.