Not CRISPR data: the image illustrates antibody quality for visualizing CRISPR experiment results.
Not CRISPR data: the image illustrates antibody quality for visualizing CRISPR experiment results.
TGF beta 1 Lentiviral Activation Particles (h): sc-400067-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- TGF beta 1 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
- TGF beta 1 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 TGF beta 1 Lentiviral Activation Plasmid (h) and TGF beta 1 Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the TGFB1 promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: TGF beta 1 Antibody (3C11): sc-130348
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
TGF beta 1 Lentiviral Activation Particles (h) | sc-400067-LAC | 200 µl | $455.00 |
Human TGFB1 encodes transforming growth factor beta 1 (TGF-β1), a pleiotropic cytokine that regulates cell proliferation, differentiation, immune modulation, and extracellular matrix remodeling. TGF-β1 signals primarily through TGFBR1/2-driven SMAD2/3 activation with extensive crosstalk to MAPK, PI3K/AKT, and Rho GTPase pathways, shaping transcriptional programs that influence epithelial–mesenchymal transition and tissue homeostasis. Dysregulated TGFB1 activity is implicated in fibrotic remodeling, tumor microenvironment signaling, immune evasion, and chronic inflammatory states, making it a key node for mechanistic studies of cytokine-driven phenotypes. Experimental modulation of TGFB1 is commonly used to interrogate pathway-dependent changes in cell fate decisions, matrix deposition, and paracrine signaling networks.
TGF beta 1 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 TGFB1 upregulation across a broader range of human cell types.
TGF beta 1 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 TGFB1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous TGF beta 1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native TGFB1 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.