PLP-J CRISPR Activation Plasmid (m2): sc-424243-ACT-2

Mouse Prl3c1 encodes the prolactin family member PLP-J, a secreted placenta-enriched protein implicated in maternal–fetal interface biology and endocrine regulation during gestation. PLP-J is studied in the context of prolactin/placental lactogen signaling networks, influencing trophoblast differentiation, decidual remodeling, and reproductive tissue cross-talk that coordinates implantation and placental development. Dysregulation of prolactin-family gene expression is associated with aberrant placentation and pregnancy-related pathophysiology, making Prl3c1 a relevant target for mechanistic studies of reproductive disorders. Prl3c1-focused gene editing and functional assays support applications in mouse models to interrogate placental signaling, lineage specification, and transcriptomic programs controlling pregnancy adaptation.

PLP-J CRISPR Activation Plasmid (m2) provides a targeted, non-destructive approach to upregulating endogenous Prl3c1 expression without altering the underlying DNA sequence.

PLP-J CRISPR Activation Plasmid (m2) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the Prl3c1 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 Prl3c1 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous PLP-J expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native Prl3c1 locus and enabling the study of PLP-J-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of PLP-J pathway restoration in tumor cells with silenced or reduced Prl3c1 expression.

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