USP25 Lentiviral Activation Particles (m): sc-424423-LAC

Mouse Usp25 encodes USP25, a deubiquitinating enzyme that removes ubiquitin chains from substrate proteins to regulate their stability, trafficking, and signal transduction. USP25 participates in ubiquitin-dependent control of inflammatory and innate immune pathways, including modulation of NF-κB and interferon-associated signaling nodes, and contributes to proteostasis by shaping turnover of pathway effectors. Altered USP25 activity has been linked in the literature to dysregulated immune responses and neuroinflammatory processes, with relevance to mechanisms studied in infection biology, neurodegeneration, and tumor-associated signaling contexts. These properties make Usp25 a useful locus for dissecting ubiquitin editing in stress responses, cytokine signaling, and cell-state regulation in mouse model systems.

USP25 Lentiviral Activation Particles (m) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient Usp25 upregulation across a broader range of human cell types.

USP25 Lentiviral Activation Particles (m) deliver all functional components of the synergistic activation mediator (SAM) system via lentiviral transduction. The system comprises three particle preparations co-transduced into target cells: one encoding catalytically inactive dCas9 (D10A and N863A mutations) fused to the VP64 transactivation domain with a blasticidin resistance gene; one encoding the MS2-p65-HSF1 fusion protein with a hygromycin resistance gene; and one encoding a target-specific 20 nt sgRNA fused to two MS2 RNA aptamers with a puromycin resistance gene. Following lentiviral transduction and genomic integration of the expression cassettes, the SAM components are stably expressed and assemble at the target locus within the proximal promoter region upstream of the Usp25 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous USP25 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Usp25 genomic locus and regulatory architecture.

The lentiviral format offers several practical advantages: stable genomic integration supports heritable activation across cell divisions; high-titer particle preparations eliminate the need for in-house viral production; and compatibility with primary, non-dividing, and transfection-resistant cell types expands experimental accessibility. Successful transduction can be confirmed and enriched through triple antibiotic selection using puromycin, hygromycin, and blasticidin.

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