bradykinin B2 R CRISPR Activation Plasmid (m): sc-419318-ACT

Mouse Bdkrb2 encodes the bradykinin B2 receptor (bradykinin B2 R), a constitutively expressed GPCR that mediates responses to kinins in vascular and inflammatory tissues. Upon ligand binding, it couples primarily to Gαq/11 and Gαi/o to activate PLCβ, elevate intracellular Ca2+, stimulate PKC, and engage nitric oxide and prostaglandin signaling that regulate vasodilation, vascular permeability, and smooth muscle tone. Bdkrb2-dependent signaling intersects with MAPK and NF-κB-linked programs that shape leukocyte recruitment, edema formation, and pain sensitization. Dysregulated B2 receptor activity is frequently studied in models of cardiovascular homeostasis, neurogenic inflammation, and renal physiology, where it can influence tissue remodeling and inflammatory burden.

bradykinin B2 R CRISPR Activation Plasmid (m) provides a targeted, non-destructive approach to upregulating endogenous Bdkrb2 expression without altering the underlying DNA sequence.

bradykinin B2 R CRISPR Activation Plasmid (m) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the Bdkrb2 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 Bdkrb2 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous bradykinin B2 R expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native Bdkrb2 locus and enabling the study of bradykinin B2 R-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of bradykinin B2 R pathway restoration in tumor cells with silenced or reduced Bdkrb2 expression.

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