
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
β-Amyloid CRISPR Activation Plasmid (h) | sc-400520-ACT | 20 µg | $397.00 |
APP encodes the amyloid precursor protein, a type I transmembrane glycoprotein that undergoes sequential cleavage by α-, β-, and γ-secretases to generate peptides including β-Amyloid. APP processing influences endosomal trafficking, synaptic function, and neuronal activity, and is integrated with vesicle transport and proteostasis pathways. Dysregulated production or clearance of β-Amyloid is strongly associated with Alzheimer’s disease-related pathology and is widely studied in the context of neuroinflammation, oxidative stress, and amyloidogenic signaling cascades. Human APP and β-Amyloid also serve as key molecular readouts for investigating secretase activity, membrane microdomain biology, and neuronal stress responses.
β-Amyloid CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous APP expression without altering the underlying DNA sequence.
β-Amyloid CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the APP 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 APP transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous β-Amyloid expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native APP locus and enabling the study of β-Amyloid-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of β-Amyloid pathway restoration in tumor cells with silenced or reduced APP expression.
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.