AMPK alpha 1 Lentiviral Activation Particles (m2): sc-430618-LAC-2

Mouse Prkaa1 encodes the catalytic AMPK alpha 1 subunit, a central energy sensor that forms the heterotrimeric AMPK complex and becomes activated by phosphorylation under low-energy conditions to coordinate metabolic adaptation. AMPKα1 regulates glucose uptake, fatty acid oxidation, autophagy, and mitochondrial homeostasis through pathways including mTORC1 inhibition and ULK1-mediated autophagy initiation, integrating signals from LKB1 and CaMKK2. Dysregulated Prkaa1/AMPK signaling is implicated in metabolic inflammation, insulin resistance, hepatic steatosis, and altered tumor cell metabolism, linking cellular energy stress responses to disease-relevant phenotypes. Gene editing of Prkaa1 in mouse models supports mechanistic studies of nutrient sensing, immunometabolic reprogramming, and cell growth control across tissues and primary cell systems.

AMPK alpha 1 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 Prkaa1 upregulation across a broader range of human cell types.

AMPK alpha 1 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 Prkaa1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous AMPK alpha 1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Prkaa1 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.