
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
MMP-3 CRISPR Activation Plasmid (h) | sc-400727-ACT | 20 µg | $397.00 |
Human MMP3 encodes matrix metalloproteinase-3 (MMP-3, stromelysin-1), a secreted zinc-dependent endopeptidase that remodels the extracellular matrix by cleaving proteoglycans, fibronectin, laminin, and additional matrix components. MMP-3 can also activate other MMP zymogens, amplifying proteolytic cascades that influence cell migration, tissue repair, angiogenesis, and inflammatory signaling within the extracellular milieu. Its expression is regulated downstream of cytokine- and growth factor–responsive pathways, including NF-κB and AP-1/MAPK programs, linking matrix turnover to immune and stromal activation states. Dysregulated MMP3 activity has been associated with pathological matrix remodeling observed in arthritis, cardiovascular disease, fibrosis, and tumor invasion biology, making it a widely used marker and mechanistic node in microenvironment-focused research.
MMP-3 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous MMP3 expression without altering the underlying DNA sequence.
MMP-3 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the MMP3 locus in human cell lines. The system is built around a catalytically inactive Cas9 (dCas9) carrying two inactivating mutations (D10A and N863A) that eliminate nuclease activity while preserving DNA binding. This dCas9 is fused to VP64, a potent transcriptional activator, and is co-expressed with a blasticidin resistance gene for selection. The second plasmid encodes the MS2-p65-HSF1 fusion protein, a secondary activator complex that works in concert with dCas9-VP64, alongside a hygromycin resistance gene. The third plasmid encodes a target-specific 20 nt sgRNA fused to two MS2 RNA aptamers that recruit the MS2-p65-HSF1 complex to the activation site, accompanied by a puromycin resistance gene. The three plasmids are delivered at a 1:1:1 mass ratio for balanced expression of all system components.
Once assembled at the target locus, the SAM complex binds within approximately 200 bp upstream of the MMP3 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous MMP-3 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native MMP3 locus and enabling the study of MMP-3-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of MMP-3 pathway restoration in tumor cells with silenced or reduced MMP3 expression.
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.