BMPR-IA CRISPR Activation Plasmid (h): sc-400581-ACT

BMPR1A encodes bone morphogenetic protein receptor type IA (BMPR-IA), a serine/threonine kinase receptor that transduces BMP ligand signals to regulate cell fate decisions, tissue patterning, and homeostatic control of proliferation and differentiation. Upon ligand binding with type II BMP receptors, BMPR-IA activates canonical SMAD1/5/9 signaling and intersects with non-canonical MAPK pathways to shape transcriptional programs in diverse cell types. BMPR1A activity is central to developmental and regenerative processes, particularly in epithelial and mesenchymal lineages, and contributes to context-dependent regulation of stem/progenitor cell behavior. Dysregulated BMP/BMPR1A signaling has been implicated in congenital anomalies and cancer-related phenotypes through altered differentiation and growth control.

BMPR-IA CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous BMPR1A expression without altering the underlying DNA sequence.

BMPR-IA CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the BMPR1A 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 BMPR1A transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous BMPR-IA expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native BMPR1A locus and enabling the study of BMPR-IA-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of BMPR-IA pathway restoration in tumor cells with silenced or reduced BMPR1A expression.

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