Cox-2 Lentiviral Activation Particles (h): sc-400072-LAC

PTGS2 encodes cyclooxygenase-2 (COX-2), an inducible, rate-limiting enzyme that converts arachidonic acid into prostaglandin H2, thereby controlling downstream prostaglandin and thromboxane biosynthesis. COX-2 expression is rapidly upregulated by inflammatory cytokines, growth factors, and microbial signals through pathways including NF-κB, MAPK, and JAK/STAT, linking stimulus-dependent transcriptional programs to lipid mediator production. By shaping prostaglandin-driven signaling, COX-2 influences vascular tone, platelet–endothelium interactions, pain and fever responses, and tissue remodeling. Dysregulated PTGS2/COX-2 activity is widely used as a molecular readout in models of chronic inflammation, tumor-associated inflammation, neuroinflammation, and cardiovascular pathophysiology.

Cox-2 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 PTGS2 upregulation across a broader range of human cell types.

Cox-2 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 PTGS2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Cox-2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native PTGS2 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.