ETAR Lentiviral Activation Particles (m): sc-420111-LAC
- Target species: mouse
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- ETAR Lentiviral Activation Particles (m) is a synergistic activation mediator (SAM) transcription activation system designed to specifically and efficiently upregulate gene expression via lentiviral transduction of cells
- ETAR Lentiviral Activation Particles (m) 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 ETAR Lentiviral Activation Plasmid (m) and ETAR Lentiviral Activation Plasmid (m2) target distinct regulatory regions of the Ednra promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: ETAR Antibody (D-2): sc-518060
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
ETAR Lentiviral Activation Particles (m) | sc-420111-LAC | 200 µl | $455.00 |
Mouse Ednra encodes endothelin receptor type A (ETAR), a G protein–coupled receptor that preferentially binds endothelin-1 to regulate vasoconstriction, smooth muscle proliferation, and extracellular matrix remodeling. ETAR signaling primarily couples to Gq/11 to activate phospholipase C, Ca2+ mobilization, and PKC, with downstream engagement of MAPK/ERK, RhoA/ROCK, and PI3K/AKT pathways that shape vascular tone and tissue remodeling. In development, Ednra is essential for neural crest–derived craniofacial and cardiovascular patterning, and its dysregulation is used to model mechanisms underlying pulmonary hypertension, fibrosis, and vascular inflammatory remodeling. These features make Ednra/ETAR a useful node for studying GPCR signal integration, contractile gene programs, and endothelin pathway cross-talk in endothelial, smooth muscle, and stromal cell systems.
ETAR Lentiviral Activation Particles (m) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient Ednra upregulation across a broader range of human cell types.
ETAR Lentiviral Activation Particles (m) 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 Ednra transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous ETAR expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Ednra 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.