CD26 Lentiviral Activation Particles (h): sc-400862-LAC

Human DPP4 encodes CD26, a type II transmembrane glycoprotein with dipeptidyl peptidase activity that truncates select incretin hormones, chemokines, and neuropeptides, shaping peptide-mediated signaling in immune and metabolic tissues. Beyond its enzymatic role, CD26 participates in co-stimulatory signaling on T cells and modulates cell–cell and cell–matrix interactions through binding partners such as adenosine deaminase and extracellular matrix components. DPP4/CD26 intersects with pathways governing inflammation, chemotaxis, and glucose homeostasis, and its expression is dynamically regulated across epithelial, endothelial, and hematopoietic compartments. Altered DPP4 activity or CD26 expression has been associated with immune dysregulation, cardiometabolic traits, and tumor biology, supporting its use as a mechanistic node in pathway-centric studies.

CD26 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 DPP4 upregulation across a broader range of human cell types.

CD26 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 DPP4 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous CD26 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native DPP4 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.