
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
LONP1 Lentiviral Activation Particles (m) | sc-428748-LAC | 200 µl | $455.00 |
Lonp1 encodes LONP1, an ATP-dependent serine protease of the mitochondrial matrix that couples protein quality control to organelle proteostasis. LONP1 recognizes and degrades oxidized or misfolded mitochondrial proteins, supports turnover of respiratory chain components, and contributes to maintenance of mtDNA and mitochondrial ribosome function under stress. Through its roles in mitochondrial unfolded protein response signaling, oxidative phosphorylation, and redox homeostasis, altered LONP1 activity is linked to mitochondrial dysfunction phenotypes affecting energy metabolism and cellular stress tolerance. In mouse systems, Lonp1 is frequently studied in contexts where mitochondrial proteostasis intersects with neurodegeneration, cardiometabolic remodeling, and aging-related declines in mitochondrial function.
LONP1 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 Lonp1 upregulation across a broader range of human cell types.
LONP1 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 Lonp1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous LONP1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Lonp1 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.