CEACAM1 Lentiviral Activation Particles (m): sc-424008-LAC
- Target species: mouse
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- CEACAM1 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
- CEACAM1 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 CEACAM1 Lentiviral Activation Plasmid (m) and CEACAM1 Lentiviral Activation Plasmid (m2) target distinct regulatory regions of the Ceacam1 promoter. One or both designs may be available
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
CEACAM1 Lentiviral Activation Particles (m) | sc-424008-LAC | 200 µl | $455.00 |
Ceacam1 encodes the mouse carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1), an immunoglobulin superfamily receptor that mediates homophilic and heterophilic cell–cell interactions and integrates signaling through its cytoplasmic ITIM/ITAM-like motifs. CEACAM1 participates in regulation of epithelial organization, endothelial barrier function, and leukocyte activation, influencing pathways linked to cell adhesion dynamics, phosphatase recruitment, and immune checkpoint-like signaling. In murine models, altered CEACAM1 activity has been associated with modulation of inflammatory responses, metabolic homeostasis, and tissue remodeling, providing relevance to studies of cancer-associated microenvironments, infection biology, and immune regulation. Its expression across hematopoietic and parenchymal compartments makes it a useful node for dissecting cross-talk between adhesion signaling and cytokine-driven responses.
CEACAM1 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 Ceacam1 upregulation across a broader range of human cell types.
CEACAM1 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 Ceacam1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous CEACAM1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Ceacam1 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.