NOS2/iNOS Lentiviral Activation Particles (m): sc-421928-LAC

Nos2 encodes inducible nitric oxide synthase (NOS2/iNOS), an enzyme that generates nitric oxide from L-arginine during inflammatory and innate immune responses. iNOS-derived nitric oxide modulates redox signaling, antimicrobial defense, and cytokine networks, intersecting with NF-κB, JAK/STAT, and MAPK-regulated transcriptional programs in macrophages and other activated cell types. Altered Nos2 activity is widely used as a mechanistic readout in models of inflammation, infection, and oxidative stress, where nitric oxide and reactive nitrogen species influence cellular metabolism, mitochondrial function, and tissue remodeling. Dysregulated iNOS signaling has been implicated in experimental systems relevant to autoimmunity, neuroinflammation, cardiovascular dysfunction, and tumor-associated immune modulation.

NOS2/iNOS 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 Nos2 upregulation across a broader range of human cell types.

NOS2/iNOS 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 Nos2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous NOS2/iNOS expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Nos2 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.