Fibromodulin Lentiviral Activation Particles (h): sc-401610-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- Fibromodulin Lentiviral Activation Particles (h) is a synergistic activation mediator (SAM) transcription activation system designed to specifically and efficiently upregulate gene expression via lentiviral transduction of cells
- Fibromodulin Lentiviral Activation Particles (h) 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 Fibromodulin Lentiviral Activation Plasmid (h) and Fibromodulin Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the FMOD promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: Fibromodulin Antibody (H-11): sc-166406
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
Fibromodulin Lentiviral Activation Particles (h) | sc-401610-LAC | 200 µl | $455.00 |
FMOD encodes fibromodulin, a small leucine-rich proteoglycan secreted into the extracellular matrix where it binds collagens and regulates fibrillogenesis, matrix assembly, and tissue mechanics. Fibromodulin modulates signaling through growth factor pathways, including TGF-β family cues, influencing cell adhesion, migration, and differentiation programs relevant to connective tissue homeostasis. Altered FMOD expression or matrix localization has been associated with remodeling phenotypes observed in fibrosis, osteoarthritis, and tumor-associated stroma, making it a useful entry point for studying extracellular matrix–driven cellular behavior. As a matrix component with regulatory interactions, fibromodulin is frequently examined in models of wound repair, angiogenesis, and mechanotransduction.
Fibromodulin 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 FMOD upregulation across a broader range of human cell types.
Fibromodulin 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 FMOD transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Fibromodulin expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native FMOD 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.