TGase2 Lentiviral Activation Particles (h): sc-401543-LAC

Human TGM2 encodes transglutaminase 2 (TGase2), a multifunctional Ca2+-dependent enzyme that catalyzes protein crosslinking and also exhibits GTPase, protein disulfide isomerase, and scaffolding activities. TGase2 coordinates extracellular matrix remodeling, cytoskeletal organization, and cell adhesion, and it modulates stress and inflammatory signaling through pathways that intersect with NF-κB, TGF-β, and integrin-mediated signaling. By influencing apoptosis, autophagy, and epithelial–mesenchymal transition-like programs, TGM2 is frequently studied in contexts of fibrosis, chronic inflammation, and tumor microenvironment adaptation. These properties make TGase2 a relevant node for mechanistic studies of proteostasis, redox balance, and matrix-associated signaling in human cells.

TGase2 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 TGM2 upregulation across a broader range of human cell types.

TGase2 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 TGM2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous TGase2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native TGM2 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.