R-Spondin2 Lentiviral Activation Particles (h): sc-402648-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- R-Spondin2 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
- R-Spondin2 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 R-Spondin2 Lentiviral Activation Plasmid (h) and R-Spondin2 Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the RSPO2 promoter. One or both designs may be available
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
R-Spondin2 Lentiviral Activation Particles (h) | sc-402648-LAC | 200 µl | $455.00 |
Human RSPO2 encodes R-Spondin2, a secreted matricellular ligand that potentiates canonical WNT/β-catenin signaling by binding LGR4/5/6 receptors and antagonizing the ubiquitin ligases RNF43/ZNRF3, thereby stabilizing Frizzled receptors at the cell surface. Through this mechanism, R-Spondin2 regulates epithelial stem cell maintenance, proliferation, and tissue morphogenesis, with downstream effects on transcriptional programs controlling differentiation and cell fate. RSPO2 activity intersects with pathways governing extracellular matrix remodeling and developmental patterning, and altered expression has been linked to dysregulated WNT signaling in cancers, as well as roles in congenital and inflammatory phenotypes in experimental systems. These features make RSPO2 a useful node for dissecting WNT pathway tuning, receptor–ligand dynamics, and context-dependent signaling outputs in human cell models.
R-Spondin2 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 RSPO2 upregulation across a broader range of human cell types.
R-Spondin2 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 RSPO2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous R-Spondin2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native RSPO2 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.