DMP-1 CRISPR Activation Plasmid (h): sc-402197-ACT

DMP1 encodes dentin matrix acidic phosphoprotein 1 (DMP-1), an extracellular matrix phosphoprotein that regulates mineral deposition and phosphate homeostasis during skeletal and dental development. DMP-1 is processed into functional fragments that influence osteocyte maturation, dentinogenesis, and the organization of hydroxyapatite through interactions with calcium/phosphate and matrix components. In bone, DMP-1 is linked to osteocyte-driven signaling networks that couple matrix mineralization with phosphate-regulatory pathways, including modulation of FGF23-associated processes. Altered DMP1 expression or function is associated with disorders of bone mineral density and dentin formation, supporting its relevance in studies of mineralization biology and heritable skeletal phenotypes.

DMP-1 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous DMP1 expression without altering the underlying DNA sequence.

DMP-1 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the DMP1 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 DMP1 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous DMP-1 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native DMP1 locus and enabling the study of DMP-1-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of DMP-1 pathway restoration in tumor cells with silenced or reduced DMP1 expression.

For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.