SIK2 Lentiviral Activation Particles (h): sc-406982-LAC

SIK2 (salt-inducible kinase 2) is a serine/threonine kinase in the AMPK-related kinase family that integrates metabolic and stress cues to coordinate transcriptional and cytoskeletal programs. It modulates CREB/CRTC signaling through phosphorylation-dependent control of CRTC coactivators, linking cAMP signaling to gene expression in processes such as glucose and lipid metabolism, adipocyte function, and cell-cycle progression. SIK2 has also been implicated in centrosome regulation and mitotic control, connecting kinase signaling to proliferation and cellular fitness. Dysregulated SIK2 activity and expression have been associated with altered metabolic homeostasis and tumor-associated signaling states, making it a useful node for studying kinase-driven regulation in human cell models.

SIK2 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 SIK2 upregulation across a broader range of human cell types.

SIK2 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 SIK2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous SIK2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native SIK2 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.