
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
OTULIN CRISPR Activation Plasmid (h) | sc-407676-ACT | 20 µg | $397.00 |
OTULIN encodes a deubiquitinase that specifically cleaves Met1-linked (linear) ubiquitin chains, acting as a key negative regulator of LUBAC-driven ubiquitin signaling. By restricting linear ubiquitination of pathway components, OTULIN modulates NF-κB and innate immune signaling outputs, shaping inflammatory responses, cell survival, and stress adaptation. Altered OTULIN function can perturb ubiquitin-dependent signal termination and has been linked to dysregulated immune homeostasis and inflammatory phenotypes. As a result, OTULIN is widely studied in ubiquitin editing, receptor-proximal signaling complexes, and mechanisms that balance cytokine signaling intensity.
OTULIN CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous OTULIN expression without altering the underlying DNA sequence.
OTULIN CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the OTULIN 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 OTULIN transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous OTULIN expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native OTULIN locus and enabling the study of OTULIN-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of OTULIN pathway restoration in tumor cells with silenced or reduced OTULIN expression.
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.