
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
PAPP-A2 CRISPR Activation Plasmid (h) | sc-412949-ACT | 20 µg | $397.00 |
PAPPA2 encodes pappalysin-2 (PAPP-A2), a secreted metalloproteinase that regulates insulin-like growth factor (IGF) bioavailability by proteolytically cleaving IGF binding proteins, with strong activity toward IGFBP-3 and IGFBP-5. By modulating the release of IGF-I/IGF-II from inhibitory complexes, PAPP-A2 influences IGF receptor signaling cascades that coordinate cell growth, differentiation, and extracellular matrix–associated remodeling. This axis is integral to endocrine and paracrine control of skeletal development and metabolic homeostasis. Altered PAPPA2 function or expression has been associated with dysregulated IGF signaling and growth phenotypes, supporting its study in developmental biology and hormone-regulated pathways.
PAPP-A2 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous PAPPA2 expression without altering the underlying DNA sequence.
PAPP-A2 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the PAPPA2 locus in human cell lines. The system is built around a catalytically inactive Cas9 (dCas9) carrying two inactivating mutations (D10A and N863A) that eliminate nuclease activity while preserving DNA binding. This dCas9 is fused to VP64, a potent transcriptional activator, and is co-expressed with a blasticidin resistance gene for selection. The second plasmid encodes the MS2-p65-HSF1 fusion protein, a secondary activator complex that works in concert with dCas9-VP64, alongside a hygromycin resistance gene. The third plasmid encodes a target-specific 20 nt sgRNA fused to two MS2 RNA aptamers that recruit the MS2-p65-HSF1 complex to the activation site, accompanied by a puromycin resistance gene. The three plasmids are delivered at a 1:1:1 mass ratio for balanced expression of all system components.
Once assembled at the target locus, the SAM complex binds within approximately 200 bp upstream of the PAPPA2 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous PAPP-A2 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native PAPPA2 locus and enabling the study of PAPP-A2-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of PAPP-A2 pathway restoration in tumor cells with silenced or reduced PAPPA2 expression.
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.