AMPKγ2 Lentiviral Activation Particles (h): sc-404970-LAC

PRKAG2 encodes the γ2 regulatory subunit of AMP-activated protein kinase (AMPK), a central heterotrimeric energy sensor that couples cellular AMP/ADP:ATP ratios to metabolic reprogramming. AMPKγ2 regulates nucleotide binding and allosteric control of the catalytic complex, influencing downstream pathways that coordinate glucose uptake, fatty acid oxidation, mitochondrial homeostasis, and suppression of anabolic programs through nodes such as mTORC1 and autophagy. In human tissues, PRKAG2 is highly relevant to energy-demanding physiology and has been linked to cardiac glycogen storage and conduction abnormalities, supporting its use in mechanistic studies of metabolic and electrophysiologic coupling. Perturbing AMPKγ2 activity also informs models of stress adaptation, nutrient signaling, and organelle quality control across diverse cell types.

AMPKγ2 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 PRKAG2 upregulation across a broader range of human cell types.

AMPKγ2 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 PRKAG2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous AMPKγ2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native PRKAG2 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.