ECM2 Lentiviral Activation Particles (m): sc-436571-LAC
- Target species: mouse
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- ECM2 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
- ECM2 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 ECM2 Lentiviral Activation Plasmid (m) and ECM2 Lentiviral Activation Plasmid (m2) target distinct regulatory regions of the Ecm2 promoter. One or both designs may be available
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
ECM2 Lentiviral Activation Particles (m) | sc-436571-LAC | 200 µl | $455.00 | |||
ECM2 Lentiviral Activation Particles (m2) | sc-436571-LAC-2 | 200 µl | $455.00 |
Mouse Ecm2 encodes extracellular matrix protein 2 (ECM2), a secreted matrix-associated glycoprotein implicated in organizing the extracellular matrix and modulating cell–matrix interactions. ECM2 is linked to processes such as cell adhesion, migration, and tissue remodeling, and it can influence signaling pathways that depend on extracellular cues, including integrin-mediated and growth factor–responsive networks. Altered extracellular matrix composition and remodeling dynamics are associated with fibrosis, inflammatory microenvironments, and tumor–stroma interactions, making Ecm2 relevant for mechanistic studies of stromal biology and matrix-regulated phenotypes. In mouse model systems, ECM2 provides a tractable entry point for dissecting how matrix components shape cellular behavior in development and disease contexts.
ECM2 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 Ecm2 upregulation across a broader range of human cell types.
ECM2 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 Ecm2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous ECM2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Ecm2 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.