Pitx2 Lentiviral Activation Particles (h): sc-401426-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- Pitx2 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
- Pitx2 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 Pitx2 Lentiviral Activation Plasmid (h) and Pitx2 Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the PITX2 promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: Pitx2 Antibody (H-1): sc-390457
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
Pitx2 Lentiviral Activation Particles (h) | sc-401426-LAC | 200 µl | $455.00 |
PITX2 encodes the paired-like homeodomain transcription factor Pitx2, a key regulator of embryonic patterning and organogenesis that helps specify left–right asymmetry and coordinates development of the heart, eye, craniofacial structures, and skeletal muscle. Pitx2 integrates upstream cues from Wnt/β-catenin, TGF-β/Nodal, and retinoic acid signaling to control lineage-specific transcriptional programs, cellular differentiation, and tissue morphogenesis. Dysregulated PITX2 activity has been linked to congenital malformations and is frequently studied in contexts such as atrial development and arrhythmia susceptibility, anterior segment dysgenesis, and craniofacial phenotypes. In cancer biology, PITX2 expression and epigenetic regulation have been investigated for roles in tumor cell state transitions, invasion-associated transcriptional networks, and pathway cross-talk.
Pitx2 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 PITX2 upregulation across a broader range of human cell types.
Pitx2 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 PITX2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Pitx2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native PITX2 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.