PAPP-A2 Lentiviral Activation Particles (h): sc-412949-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- PAPP-A2 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
- PAPP-A2 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 PAPP-A2 Lentiviral Activation Plasmid (h) and PAPP-A2 Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the PAPPA2 promoter. One or both designs may be available
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
PAPP-A2 Lentiviral Activation Particles (h) | sc-412949-LAC | 200 µl | $455.00 |
PAPPA2 encodes pregnancy-associated plasma protein-A2 (PAPP-A2), a secreted metalloproteinase that cleaves insulin-like growth factor binding proteins, particularly IGFBP-3 and IGFBP-5, thereby increasing local IGF bioavailability and modulating IGF/PI3K-AKT and MAPK signaling. Through control of IGF ligand access, PAPP-A2 influences cell growth, differentiation, and extracellular microenvironment–dependent responses in multiple tissues. Genetic and functional studies associate PAPPA2 dysregulation with altered growth phenotypes and endocrine-related traits linked to IGF axis imbalance, making it relevant to investigations of development, metabolism, and tissue remodeling. Its extracellular proteolytic activity also connects PAPPA2 to studies of protease biology and secreted pathway regulation in physiological and disease-associated contexts.
PAPP-A2 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 PAPPA2 upregulation across a broader range of human cell types.
PAPP-A2 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 PAPPA2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous PAPP-A2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native PAPPA2 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.