PORCN Lentiviral Activation Particles (h): sc-413044-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- PORCN 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
- PORCN 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 PORCN Lentiviral Activation Plasmid (h) and PORCN Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the PORCN promoter. One or both designs may be available
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
PORCN Lentiviral Activation Particles (h) | sc-413044-LAC | 200 µl | $455.00 |
Human PORCN encodes a membrane-bound O-acyltransferase in the endoplasmic reticulum that catalyzes palmitoleoylation of WNT ligands, a modification required for WNT secretion, receptor engagement, and formation of WNT gradients. Through controlling WNT ligand maturation, PORCN regulates canonical β-catenin–dependent transcription as well as non-canonical WNT/planar cell polarity signaling, influencing proliferation, differentiation, polarity, and tissue patterning. Perturbation of PORCN-dependent WNT signaling is implicated in developmental disorders and in disease contexts where WNT pathway activity is dysregulated, including cancers and fibrotic remodeling. As an upstream, rate-limiting node in WNT ligand production, PORCN is a useful target for mechanistic studies of pathway output and paracrine signaling dynamics.
PORCN 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 PORCN upregulation across a broader range of human cell types.
PORCN 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 PORCN transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous PORCN expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native PORCN 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.