PRL-3 CRISPR Activation Plasmid (h): sc-402331-ACT

PTP4A3 encodes PRL-3, a prenylated protein tyrosine phosphatase that localizes to intracellular membranes and modulates phosphorylation-dependent signaling networks controlling cell migration, cytoskeletal remodeling, and proliferation. PRL-3 has been linked to regulation of pathways including PI3K/AKT, MAPK/ERK, and Rho family GTPase signaling, influencing adhesion dynamics and invasive phenotypes. Dysregulated PTP4A3/PRL-3 expression is frequently studied in the context of tumor progression and metastasis biology, where it correlates with altered survival and motility programs. As a human gene target, PTP4A3 is used to interrogate phosphatase-driven rewiring of signaling circuits and transcriptional states relevant to oncogenic transformation and microenvironmental adaptation.

PRL-3 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous PTP4A3 expression without altering the underlying DNA sequence.

PRL-3 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the PTP4A3 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 PTP4A3 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous PRL-3 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native PTP4A3 locus and enabling the study of PRL-3-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of PRL-3 pathway restoration in tumor cells with silenced or reduced PTP4A3 expression.

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