
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
USP24 CRISPR Activation Plasmid (h) | sc-411721-ACT | 20 µg | $397.00 |
Human USP24 encodes a ubiquitin-specific protease that removes ubiquitin moieties from protein substrates, shaping proteostasis by regulating substrate stability, trafficking, and signaling output. As a component of the ubiquitin–proteasome system, USP24 influences cellular stress responses, DNA damage signaling, and checkpoint control by modulating turnover of key regulatory proteins. Altered deubiquitination dynamics involving USP24 have been linked to dysregulated cell-cycle progression, aberrant apoptotic signaling, and inflammatory pathway remodeling in disease-relevant contexts. These properties make USP24 a useful target for dissecting ubiquitin-dependent control of transcriptional programs and signaling networks in human cell models.
USP24 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous USP24 expression without altering the underlying DNA sequence.
USP24 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the USP24 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 USP24 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous USP24 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native USP24 locus and enabling the study of USP24-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of USP24 pathway restoration in tumor cells with silenced or reduced USP24 expression.
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.