PHOSPHO1 Lentiviral Activation Particles (m): sc-433594-LAC
- Target species: mouse
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- PHOSPHO1 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
- PHOSPHO1 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 PHOSPHO1 Lentiviral Activation Plasmid (m) and PHOSPHO1 Lentiviral Activation Plasmid (m2) target distinct regulatory regions of the Phospho1 promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: PHOSPHO1 Antibody (II-91): sc-100351
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
PHOSPHO1 Lentiviral Activation Particles (m) | sc-433594-LAC | 200 µl | $455.00 |
Phospho1 encodes PHOSPHO1, a cytosolic phosphatase enriched in mineralizing tissues that hydrolyzes phosphoethanolamine and phosphocholine to generate inorganic phosphate for matrix vesicle–mediated hydroxyapatite formation. PHOSPHO1 functions alongside extracellular nucleotide pyrophosphatases and alkaline phosphatases to regulate the local phosphate/pyrophosphate balance that controls biomineral deposition. In mouse models, altered PHOSPHO1 activity disrupts osteoblast-driven skeletal mineralization, linking this pathway to impaired bone formation and mineral density phenotypes. This biology makes PHOSPHO1 a relevant node for studying osteogenesis programs, matrix vesicle biology, and phosphate homeostasis in musculoskeletal research.
PHOSPHO1 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 Phospho1 upregulation across a broader range of human cell types.
PHOSPHO1 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 Phospho1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous PHOSPHO1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Phospho1 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.