HXK II Lentiviral Activation Particles (m): sc-420866-LAC

Mouse Hk2 encodes hexokinase II (HXK II), a mitochondrial-associated enzyme that catalyzes the first committed step of glycolysis by phosphorylating glucose to glucose-6-phosphate, thereby linking glucose uptake to glycolytic flux and downstream biosynthetic pathways. HXK II integrates metabolic signaling with cell survival by coupling to the outer mitochondrial membrane and influencing ATP utilization, redox balance, and apoptotic susceptibility. Hk2 activity intersects with insulin/PI3K–AKT signaling, hypoxia responses, and nutrient-sensing networks that coordinate glycolysis, the pentose phosphate pathway, and anaplerotic inputs to the TCA cycle. Dysregulated HXK II expression or localization is frequently studied in models of metabolic reprogramming, inflammation, and tumor-associated glycolytic phenotypes, supporting its relevance in disease-focused mechanistic research.

HXK II 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 Hk2 upregulation across a broader range of human cell types.

HXK II 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 Hk2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous HXK II expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Hk2 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.