PPP2R3A CRISPR Activation Plasmid (h): sc-402433-ACT

PPP2R3A encodes a regulatory B″/PR72 subunit of protein phosphatase 2A (PP2A), a major serine/threonine phosphatase that shapes phospho-signaling by directing substrate recognition and subcellular targeting of the PP2A holoenzyme. Through PP2A-dependent control of kinase–phosphatase balance, PPP2R3A is implicated in coordination of cell-cycle progression, DNA damage responses, and broader signal transduction programs that influence metabolism and stress adaptation. Altered PP2A regulatory subunit composition is frequently associated with dysregulated phosphorylation networks observed in proliferative and neurobiological disorders, making PPP2R3A relevant for dissecting pathway rewiring. Modulating PPP2R3A expression is therefore useful for studying phosphatase-mediated regulation of growth and signaling nodes in human cellular models.

PPP2R3A CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous PPP2R3A expression without altering the underlying DNA sequence.

PPP2R3A CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the PPP2R3A 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 PPP2R3A transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous PPP2R3A expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native PPP2R3A locus and enabling the study of PPP2R3A-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of PPP2R3A pathway restoration in tumor cells with silenced or reduced PPP2R3A expression.

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