CIP2A CRISPR Activation Plasmid (h): sc-401363-ACT

Cancerous inhibitor of PP2A (CIP2A) encodes a human oncoprotein that inhibits the serine/threonine phosphatase PP2A, thereby sustaining phosphorylation-dependent signaling and stabilizing growth-promoting factors such as MYC. By antagonizing PP2A tumor suppressor activity, CIP2A supports proliferative and pro-survival pathways including PI3K/AKT and MAPK signaling, and contributes to altered cell cycle progression and stress responses. Elevated CIP2A expression has been reported across multiple tumor types and is associated with aggressive phenotypes and resistance-associated signaling states, making it a useful node for studying phosphatase-controlled oncogenic networks.

CIP2A CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous CIP2A expression without altering the underlying DNA sequence.

CIP2A CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the CIP2A 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 CIP2A transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous CIP2A expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native CIP2A locus and enabling the study of CIP2A-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of CIP2A pathway restoration in tumor cells with silenced or reduced CIP2A expression.

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