S-100PBP CRISPR Activation Plasmid (h2): sc-413030-ACT-2

Human S100PBP (S-100P binding protein), encoded by S100PBP, functions as an intracellular binding partner of the calcium-binding protein S100P and is implicated in coordinating Ca2+-dependent signaling with cytoskeletal organization and cell adhesion dynamics. The protein has been linked to regulation of microtubule-associated processes and may influence vesicular trafficking and cell-cycle–related events through protein–protein interaction networks that modulate cellular polarity and motility. Altered S100PBP expression patterns have been reported in multiple tumor contexts, supporting its utility for dissecting mechanisms underlying migration, invasion, and epithelial–mesenchymal transitions without implying clinical outcomes. Gene editing or perturbation of S100PBP in human cell models enables functional interrogation of S100P-centered pathways, mapping of interaction partners, and evaluation of downstream transcriptional and phenotypic effects relevant to cancer biology and cell signaling research.

S-100PBP CRISPR Activation Plasmid (h2) provides a targeted, non-destructive approach to upregulating endogenous S100PBP expression without altering the underlying DNA sequence.

S-100PBP CRISPR Activation Plasmid (h2) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the S100PBP 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 S100PBP transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous S-100PBP expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native S100PBP locus and enabling the study of S-100PBP-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of S-100PBP pathway restoration in tumor cells with silenced or reduced S100PBP expression.

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