TGFβ2 Lentiviral Activation Particles (h): sc-400496-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- TGFβ2 Lentiviral Activation Particles (h) is a synergistic activation mediator (SAM) transcription activation system designed to specifically and efficiently upregulate gene expression via lentiviral transduction of cells
- TGFβ2 Lentiviral Activation Particles (h) contain the following SAM Activation elements: a deactivated Cas9 (dCas9) nuclease (D10A and N863A) fused to the transactivation domain VP64, an MS2-p65-HSF1 fusion protein and a target-specific 20 nt guide RNA. They also contain the blasticidin, hygromycin and puromycin resistance genes
- Upon transduction, the SAM complex binds to a site-specific region approximately 200-250 nt upstream of the transcriptional start site and provides robust recruitment of transcription factors for highly efficient gene activation
- gRNAs encoded by TGFβ2 Lentiviral Activation Plasmid (h) and TGFβ2 Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the TGFB2 promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: TGFβ2 Antibody (H-6): sc-374659
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
TGFβ2 Lentiviral Activation Particles (h) | sc-400496-LAC | 200 µl | $455.00 |
TGFB2 encodes the secreted cytokine transforming growth factor beta 2 (TGFβ2), a pleiotropic regulator of cell fate decisions including proliferation, differentiation, epithelial–mesenchymal transition, and extracellular matrix production. Following activation from its latent complex, TGFβ2 signals primarily through TGF-β receptor I/II to induce SMAD2/3 phosphorylation and transcriptional programs, with additional crosstalk to MAPK, PI3K–AKT, and Rho GTPase pathways. This signaling axis shapes tissue remodeling, angiogenic responses, and immune modulation in a context-dependent manner. Dysregulated TGFB2/TGFβ2 activity is implicated in fibrotic remodeling, developmental abnormalities, and tumor microenvironment biology, making it a frequent focus in mechanistic studies of matrix homeostasis and cytokine-driven signaling.
TGFβ2 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 TGFB2 upregulation across a broader range of human cell types.
TGFβ2 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 TGFB2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous TGFβ2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native TGFB2 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.