ZPR1 CRISPR Activation Plasmid (m): sc-423774-ACT

ZPR1 (zinc finger protein ZPR1) is an evolutionarily conserved RNA-binding and zinc-finger–containing protein implicated in transcriptional control, RNA metabolism, and growth factor–responsive signaling. In mouse cells, ZPR1 participates in nuclear–cytoplasmic trafficking and associates with RNA processing complexes, linking mitogenic cues to gene expression programs that support proliferation and cellular stress responses. Functional studies connect ZPR1 to motor neuron biology and pathways relevant to spinal muscular atrophy through its relationship with SMN-associated ribonucleoprotein assembly and RNA splicing dynamics. Dysregulation of ZPR1-dependent RNA regulatory networks is therefore of interest for modeling neurodegeneration and for mechanistic studies of transcription–RNA processing coupling.

ZPR1 CRISPR Activation Plasmid (m) provides a targeted, non-destructive approach to upregulating endogenous Zpr1 expression without altering the underlying DNA sequence.

ZPR1 CRISPR Activation Plasmid (m) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the Zpr1 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 Zpr1 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous ZPR1 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native Zpr1 locus and enabling the study of ZPR1-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of ZPR1 pathway restoration in tumor cells with silenced or reduced Zpr1 expression.

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