PI 3-kinase p55γ Lentiviral Activation Particles (h): sc-402964-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- PI 3-kinase p55γ Lentiviral Activation Particles (h) is a synergistic activation mediator (SAM) transcription activation system designed to specifically and efficiently upregulate gene expression via lentiviral transduction of cells
- PI 3-kinase p55γ Lentiviral Activation Particles (h) 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 PI 3-kinase p55γ Lentiviral Activation Plasmid (h) and PI 3-kinase p55γ Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the PIK3R3 promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: PI 3-kinase p55γ Antibody (E-9): sc-376615
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
PI 3-kinase p55γ Lentiviral Activation Particles (h) | sc-402964-LAC | 200 µl | $455.00 |
PIK3R3 encodes the p55γ regulatory subunit of class IA phosphoinositide 3-kinase (PI3K), which couples activated receptor tyrosine kinases and adaptor proteins to catalytic p110 isoforms. Through modulation of PI(3,4,5)P3 production, PI3K signaling coordinates AKT–mTOR pathway activity, influencing cell growth, survival, metabolism, and cytoskeletal dynamics. Altered regulation of PI3K pathway components is frequently associated with oncogenic signaling, aberrant proliferation, and resistance to cellular stress, making PIK3R3 a relevant node for pathway dissection. In immune and epithelial contexts, p55γ-dependent PI3K outputs can also shape motility and signaling crosstalk that impact inflammatory and tumor-associated microenvironmental programs.
PI 3-kinase p55γ 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 PIK3R3 upregulation across a broader range of human cell types.
PI 3-kinase p55γ 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 PIK3R3 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous PI 3-kinase p55γ expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native PIK3R3 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.