PTPμ CRISPR Activation Plasmid (h): sc-403126-ACT

PTPRM encodes receptor-type protein tyrosine phosphatase mu (PTPμ), a single-pass transmembrane phosphatase that mediates homophilic cell–cell adhesion and couples extracellular contacts to intracellular tyrosine dephosphorylation. Through regulation of cadherin–catenin complexes and junctional substrates, PTPμ influences epithelial and endothelial barrier function, cell migration, and cytoskeletal organization. PTPRM activity intersects with receptor tyrosine kinase signaling and downstream pathways such as MAPK and PI3K/AKT by tuning phosphorylation-dependent signaling thresholds. Altered PTPRM expression or phosphorylation control has been associated with dysregulated adhesion and invasive phenotypes in multiple disease-relevant contexts, making it a useful node for mechanistic studies of tissue organization and signaling balance.

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

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

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