TIF1α Lentiviral Activation Particles (h): sc-403838-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- TIF1α 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
- TIF1α 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 TIF1α Lentiviral Activation Plasmid (h) and TIF1α Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the TRIM24 promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: TIF1α Antibody (C-4): sc-271266
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
TIF1α Lentiviral Activation Particles (h) | sc-403838-LAC | 200 µl | $455.00 |
TRIM24 (TIF1α) encodes a transcriptional co-regulator with E3 ubiquitin ligase activity that integrates chromatin cues through a C3HC4 RING domain and PHD-bromodomain module to modulate gene expression programs. TIF1α participates in nuclear receptor signaling and broader epigenetic control of transcription, influencing processes such as cell-cycle progression, DNA damage responses, and chromatin remodeling. Through context-dependent interactions with transcription factors and histone marks, TRIM24 can shape oncogenic and differentiation-associated pathways, making it a frequently studied node in cancer biology and transcriptional regulation. Dysregulated TRIM24 activity or expression has been linked to altered proliferative and metabolic transcriptional states, supporting its relevance for mechanistic studies of gene regulatory networks.
TIF1α 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 TRIM24 upregulation across a broader range of human cell types.
TIF1α 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 TRIM24 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous TIF1α expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native TRIM24 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.