HEATR5B Lentiviral Activation Particles (h2): sc-412293-LAC-2
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- HEATR5B 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
- HEATR5B 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 HEATR5B Lentiviral Activation Plasmid (h2) and HEATR5B Lentiviral Activation Plasmid (h22) target distinct regulatory regions of the HEATR5B promoter. One or both designs may be available
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
HEATR5B Lentiviral Activation Particles (h2) | sc-412293-LAC-2 | 200 µl | $455.00 |
Human HEATR5B encodes a HEAT repeat–containing protein thought to function as a scaffold for protein–protein interactions that support coordinated macromolecular complex assembly and intracellular organization. Based on conserved HEAT-repeat biology, HEATR5B is expected to influence processes such as nucleocytoplasmic transport, cytoskeletal dynamics, and regulation of signaling and cell cycle–linked pathways by modulating the localization and stability of partner proteins. Altered expression or variation in HEAT-repeat scaffolding factors is frequently associated with disrupted proteostasis and cellular stress responses, mechanisms relevant to proliferative and neurodevelopmental disease biology. HEATR5B perturbation models are therefore useful for interrogating pathway connectivity, mapping interaction networks, and assessing downstream transcriptomic and phenotypic consequences in human cell systems.
HEATR5B 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 HEATR5B upregulation across a broader range of human cell types.
HEATR5B 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 HEATR5B transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous HEATR5B expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native HEATR5B 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.