DRIM CRISPR Activation Plasmid (h): sc-409900-ACT

UTP20 encodes DRIM, a nucleolar ribosome biogenesis factor required for maturation of the 18S rRNA and assembly of the small ribosomal subunit. DRIM participates in preribosomal RNA processing and nucleolar organization, linking rRNA synthesis to cell growth control and global translational capacity. Dysregulation of ribosome biogenesis and nucleolar stress pathways is broadly associated with proliferative phenotypes and altered proteostasis, making UTP20/DRIM relevant to studies of growth signaling, cell cycle progression, and stress-adaptive transcriptional programs. As a core component of fundamental RNA processing machinery, DRIM perturbation provides a mechanistic entry point for dissecting ribosomopathy-related molecular signatures in human cellular models.

DRIM CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous UTP20 expression without altering the underlying DNA sequence.

DRIM CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the UTP20 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 UTP20 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous DRIM expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native UTP20 locus and enabling the study of DRIM-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of DRIM pathway restoration in tumor cells with silenced or reduced UTP20 expression.

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