SNRPC CRISPR Activation Plasmid (h): sc-404002-ACT

SNRPC encodes the U1 small nuclear ribonucleoprotein C, a core component of the U1 snRNP within the spliceosome that recognizes 5′ splice sites and promotes early spliceosome assembly. By stabilizing U1 snRNA interactions at pre-mRNA junctions, SNRPC supports accurate intron removal and influences alternative splicing patterns that shape transcript diversity. Perturbation of U1 snRNP function can lead to widespread splicing defects, altered gene expression programs, and cellular stress responses linked to dysregulated RNA processing. As a central RNA-binding splicing factor, SNRPC is frequently studied in pathways governing mRNA maturation, nuclear RNP dynamics, and transcriptome integrity in disease-relevant models.

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

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

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