MAVS Lentiviral Activation Particles (h): sc-400769-LAC

Human MAVS (mitochondrial antiviral-signaling protein) is a mitochondria-associated adaptor essential for sensing cytosolic viral RNA and initiating innate immune defense. Upon activation by RIG-I (DDX58) and MDA5 (IFIH1), MAVS assembles prion-like signaling complexes that propagate through TRAF-dependent pathways to activate TBK1/IKKε and the IKK complex, culminating in IRF3/IRF7- and NF-κB-driven type I interferon and inflammatory gene programs. MAVS signaling intersects with mitochondrial dynamics, apoptosis, and metabolic stress responses, linking organelle homeostasis to antiviral transcriptional remodeling. Dysregulated MAVS pathway activity has been implicated in altered antiviral responsiveness, chronic inflammation, and immune evasion mechanisms relevant to infection biology and inflammation-associated disease models.

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

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