AMPKβ2 Lentiviral Activation Particles (h): sc-403537-LAC

PRKAB2 encodes the β2 regulatory subunit of AMP-activated protein kinase (AMPK), a central energy-sensing complex that integrates cellular ATP/AMP status to coordinate metabolic homeostasis. AMPKβ2 helps scaffold the heterotrimeric kinase and contributes to substrate targeting and complex stability, thereby influencing downstream programs such as fatty acid oxidation, glucose uptake, autophagy, and inhibition of anabolic signaling through pathways including mTOR. In human tissues, AMPK signaling intersects with mitochondrial function and stress responses, linking PRKAB2 regulation to phenotypes relevant to metabolic adaptation and cellular survival under nutrient limitation. Altered AMPK pathway activity has been studied in contexts such as insulin resistance, obesity-associated metabolic dysfunction, and tumor cell metabolic reprogramming, supporting PRKAB2 as a mechanistic node in energy homeostasis research.

AMPKβ2 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 PRKAB2 upregulation across a broader range of human cell types.

AMPKβ2 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 PRKAB2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous AMPKβ2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native PRKAB2 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.