COMMD1 CRISPR Activation Plasmid (h): sc-404544-ACT

COMMD1 (copper metabolism domain containing 1) is a multifunctional human adaptor protein that coordinates ubiquitin-dependent signaling and protein trafficking. It is best known for modulating NF-κB transcriptional output through interactions with the IKK complex and Cullin-RING ubiquitin ligases, thereby shaping inflammatory and stress-response gene programs. COMMD1 also contributes to endosomal sorting and membrane protein turnover, with downstream effects on pathways such as hypoxia signaling and metal ion homeostasis. Dysregulated COMMD1 activity has been associated with altered inflammatory signaling, perturbations in copper handling, and phenotypes relevant to cancer biology and hepatocellular function in experimental systems.

COMMD1 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous COMMD1 expression without altering the underlying DNA sequence.

COMMD1 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the COMMD1 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 COMMD1 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous COMMD1 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native COMMD1 locus and enabling the study of COMMD1-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of COMMD1 pathway restoration in tumor cells with silenced or reduced COMMD1 expression.

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