EphA7 Lentiviral Activation Particles (h2): sc-401722-LAC-2

Human EPHA7 encodes the EphA7 receptor tyrosine kinase, a membrane-bound ephrin receptor that mediates contact-dependent signaling to regulate cell positioning, axon guidance, and tissue boundary formation during development. EphA7 activation by ephrin-A ligands triggers bidirectional signaling and downstream pathways including Rho family GTPase control of cytoskeletal dynamics and modulation of MAPK/ERK and PI3K/AKT networks, influencing adhesion, migration, and proliferation. Dysregulated EPHA7 expression or signaling has been linked to altered neurodevelopmental circuitry and to oncogenic processes such as disrupted growth control and invasive behavior in multiple tumor contexts. EPHA7 gene editing and functional genomics tools support mechanistic studies of ephrin–Eph signaling, receptor phosphorylation and trafficking, and pathway crosstalk in neuronal models, organoids, and cancer cell systems.

EphA7 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 EPHA7 upregulation across a broader range of human cell types.

EphA7 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 EPHA7 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous EphA7 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native EPHA7 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.