EphB6 Lentiviral Activation Particles (m): sc-420202-LAC
- Target species: mouse
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- EphB6 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
- EphB6 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 EphB6 Lentiviral Activation Plasmid (m) and EphB6 Lentiviral Activation Plasmid (m2) target distinct regulatory regions of the Ephb6 promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: EphB6 Antibody (D-7): sc-398795
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
EphB6 Lentiviral Activation Particles (m) | sc-420202-LAC | 200 µl | $455.00 |
Mouse Ephb6 encodes EphB6, an atypical Eph receptor tyrosine kinase family member with impaired catalytic activity that modulates ephrin-B–dependent cell–cell communication. Through interactions with other Eph receptors and ephrin ligands, EphB6 contributes to contact-dependent signaling that influences cytoskeletal remodeling, adhesion, and migration, with downstream effects on pathways such as Rho family GTPase signaling and MAPK/ERK dynamics. Ephb6 is studied in contexts including immune cell activation and epithelial organization, where altered Eph/ephrin signaling can reshape tissue architecture and inflammatory microenvironments. Dysregulated EphB6-associated signaling has been linked to changes in tumor cell behavior and metastatic potential in experimental models, supporting its relevance for mechanistic studies of disease-associated cellular phenotypes.
EphB6 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 Ephb6 upregulation across a broader range of human cell types.
EphB6 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 Ephb6 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous EphB6 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Ephb6 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.