ICAM-1/CD54 Lentiviral Activation Particles (h): sc-400098-LAC

Intercellular adhesion molecule 1 (ICAM1), also known as ICAM-1/CD54, is an immunoglobulin superfamily cell-surface glycoprotein that mediates firm leukocyte adhesion and transmigration through binding to integrins such as LFA-1 (ITGAL/ITGB2) and Mac-1 (ITGAM/ITGB2). Its expression is strongly induced by inflammatory cytokines and pattern-recognition signaling, integrating inputs from NF-κB and MAPK pathways to regulate endothelial activation and immune cell trafficking. ICAM-1 also participates in cytoskeletal remodeling and outside-in signaling that can influence barrier function and cell–cell interactions. Dysregulated ICAM1 expression is associated with chronic inflammation, vascular pathology, autoimmune phenotypes, and tumor-associated immune microenvironment dynamics, making it a useful node for mechanistic studies of inflammation and adhesion biology.

ICAM-1/CD54 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 ICAM1 upregulation across a broader range of human cell types.

ICAM-1/CD54 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 ICAM1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous ICAM-1/CD54 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native ICAM1 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.