Mfn2/Mitofusin 2 Lentiviral Activation Particles (h): sc-400536-LAC

MFN2 encodes mitofusin 2 (Mfn2), a dynamin-like GTPase on the outer mitochondrial membrane that mediates mitochondrial fusion and helps maintain mitochondrial network architecture. Beyond fusion, Mfn2 contributes to mitochondrial–endoplasmic reticulum contact sites, influencing calcium exchange, lipid transfer, and coordination of oxidative phosphorylation with cellular energy demands. Through these roles, MFN2 impacts mitophagy, redox homeostasis, and stress-response signaling pathways that shape cell survival and metabolic adaptation. Dysregulated MFN2 activity has been associated with neuropathy and broader mitochondrial dysfunction phenotypes, making it a useful target for studying organelle dynamics in disease-relevant models.

Mfn2/Mitofusin 2 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 MFN2 upregulation across a broader range of human cell types.

Mfn2/Mitofusin 2 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 MFN2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Mfn2/Mitofusin 2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native MFN2 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.