SLAM Lentiviral Activation Particles (h): sc-404289-LAC

Human SLAMF1 encodes SLAM (CD150), an immunoglobulin superfamily receptor expressed primarily on hematopoietic cells, including activated T cells, B cells, dendritic cells, and macrophages. SLAM functions as a self-ligand that signals through immunoreceptor tyrosine-based switch motifs to recruit adaptor proteins such as SH2D1A/SAP and EAT-2, shaping downstream pathways that regulate lymphocyte activation, cytokine production, cytotoxicity, and germinal center responses. Through modulation of immune synapse organization and NF-κB/MAPK-linked signaling programs, SLAM contributes to coordination of adaptive and innate immune communication. Altered SLAMF1 signaling has been associated with immune dysregulation phenotypes and is frequently studied in the context of infection biology, inflammatory responses, and hematologic malignancy mechanisms.

SLAM 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 SLAMF1 upregulation across a broader range of human cell types.

SLAM 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 SLAMF1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous SLAM expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native SLAMF1 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.