PPP1R26 CRISPR Activation Plasmid (h): sc-411368-ACT

PPP1R26 encodes a regulatory protein that associates with protein phosphatase 1 (PP1) complexes, helping direct phosphatase activity toward specific substrates and subcellular compartments. Through modulation of serine/threonine dephosphorylation, PPP1R26 is positioned to influence phosphorylation-dependent programs including cell-cycle progression, chromatin-associated processes, and transcriptional control. Perturbation of PP1 regulatory networks can reshape signaling fidelity and proteostasis, making PPP1R26 relevant to studies of aberrant phosphoregulation observed across diverse disease contexts. Its expression and interaction dynamics provide a useful handle for dissecting how PP1 targeting contributes to cellular state transitions.

PPP1R26 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous PPP1R26 expression without altering the underlying DNA sequence.

PPP1R26 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the PPP1R26 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 PPP1R26 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous PPP1R26 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native PPP1R26 locus and enabling the study of PPP1R26-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of PPP1R26 pathway restoration in tumor cells with silenced or reduced PPP1R26 expression.

For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.