USP45 Lentiviral Activation Particles (m2): sc-429548-LAC-2

Mouse Usp45 encodes the deubiquitinating enzyme USP45, a ubiquitin-specific protease that regulates protein turnover by removing ubiquitin chains and thereby modulating the stability and activity of key nuclear substrates. USP45 has been implicated in genome maintenance through roles in DNA repair and replication-associated stress responses, linking it to pathways that preserve chromatin integrity and coordinate cell-cycle progression. Dysregulated deubiquitination and impaired DNA damage handling associated with USP45 perturbation are relevant to studies of genomic instability phenotypes and cancer-associated mechanisms. Usp45/USP45 research tools support investigations into ubiquitin signaling, DNA damage response network mapping, and functional genomics in mouse cell and in vivo models.

USP45 Lentiviral Activation Particles (m2) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient Usp45 upregulation across a broader range of human cell types.

USP45 Lentiviral Activation Particles (m2) 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 Usp45 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous USP45 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Usp45 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.