PRMT1 CRISPR Activation Plasmid (h): sc-402249-ACT

PRMT1 (protein arginine methyltransferase 1) is the predominant type I PRMT in human cells, catalyzing asymmetric dimethylation of arginine residues on histones and numerous non-histone substrates. Through these post-translational modifications, PRMT1 regulates chromatin accessibility, transcriptional programs, RNA processing, DNA damage responses, and signal transduction, with notable connections to MAPK/ERK and PI3K/AKT pathway outputs via methylation-dependent protein interactions. PRMT1 activity shapes cell-cycle progression, differentiation states, and stress adaptation by coordinating epigenetic and post-transcriptional control. Dysregulated PRMT1 expression or substrate methylation patterns are frequently studied in cancer biology, immune signaling, and neurobiology as molecular correlates of altered gene expression and proteome function.

PRMT1 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous PRMT1 expression without altering the underlying DNA sequence.

PRMT1 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the PRMT1 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 PRMT1 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous PRMT1 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native PRMT1 locus and enabling the study of PRMT1-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of PRMT1 pathway restoration in tumor cells with silenced or reduced PRMT1 expression.

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