TP53INP2 Lentiviral Activation Particles (h2): sc-405261-LAC-2
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- TP53INP2 Lentiviral Activation Particles (h2) is a synergistic activation mediator (SAM) transcription activation system designed to specifically and efficiently upregulate gene expression via lentiviral transduction of cells
- TP53INP2 Lentiviral Activation Particles (h2) 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 TP53INP2 Lentiviral Activation Plasmid (h2) and TP53INP2 Lentiviral Activation Plasmid (h22) target distinct regulatory regions of the TP53INP2 promoter. One or both designs may be available
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
TP53INP2 Lentiviral Activation Particles (h2) | sc-405261-LAC-2 | 200 µl | $455.00 |
Human TP53INP2 (tumor protein p53 inducible nuclear protein 2; also known as DOR) encodes a stress-responsive regulator of autophagy that functions as a scaffold for ATG protein recruitment and supports autophagosome formation and maturation. TP53INP2 participates in nutrient-sensing and transcriptional programs linked to p53 signaling and mTOR-controlled autophagy, influencing proteostasis, mitochondrial quality control, and cell survival decisions under metabolic stress. Dysregulated TP53INP2 expression or localization has been associated with altered autophagic flux in contexts relevant to cancer biology, neurodegeneration, and metabolic disorders, where impaired clearance pathways can impact genomic stability and inflammation. Gene editing of TP53INP2 enables mechanistic studies of autophagy pathway architecture, epistasis with core ATG factors, and functional genomics screens connecting stress signaling to disease-relevant cellular phenotypes.
TP53INP2 Lentiviral Activation Particles (h2) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient TP53INP2 upregulation across a broader range of human cell types.
TP53INP2 Lentiviral Activation Particles (h2) 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 TP53INP2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous TP53INP2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native TP53INP2 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.