Glycodelin CRISPR Activation Plasmid (h): sc-403687-ACT

PAEP encodes glycodelin, a secreted glycoprotein also known as progesterone-associated endometrial protein that is highly regulated by hormonal cues in reproductive tissues. Glycodelin contributes to cell–cell communication at the maternal–fetal interface, modulates immune cell activity, and influences epithelial differentiation and tissue remodeling through glycan-dependent receptor interactions. Altered PAEP expression has been reported in endometrial and ovarian biology and is frequently explored in studies of implantation, inflammation, and tumor-associated immune modulation. As a secreted factor, glycodelin is also investigated as a context-dependent biomarker candidate and as a mechanistic node linking endocrine signaling to local immune tolerance.

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

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

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