Integrin β4/ITGB4/CD104 Lentiviral Activation Particles (h): sc-400573-LAC

ITGB4 encodes integrin β4 (CD104), a laminin-binding integrin subunit that pairs predominantly with integrin α6 to form α6β4, a key adhesion receptor in epithelial cells. Through hemidesmosome assembly and linkage to intermediate filaments via plectin, ITGB4 stabilizes cell–basement membrane attachment while also participating in signaling processes that regulate polarity, survival, and migration. Outside stable adhesions, α6β4 can engage pathways such as PI3K–AKT, MAPK, and focal adhesion-associated signaling to modulate cytoskeletal remodeling and stress responses. Dysregulated ITGB4 expression or distribution is frequently examined in epithelial barrier dysfunction, tissue remodeling, and cancer cell invasion/metastatic phenotypes, making it a useful node for studying adhesion-dependent signaling and microenvironment interactions.

Integrin β4/ITGB4/CD104 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 ITGB4 upregulation across a broader range of human cell types.

Integrin β4/ITGB4/CD104 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 ITGB4 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Integrin β4/ITGB4/CD104 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native ITGB4 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.