
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
KY peptidase CRISPR Activation Plasmid (m) | sc-421366-ACT | 20 µg | $397.00 |
Mouse Ky encodes KY peptidase, a muscle-enriched protein implicated in skeletal muscle organization and maintenance of sarcomeric integrity. KY peptidase is associated with cytoskeletal remodeling and proteostasis processes that support myofiber stability, with reported links to pathways governing muscle development and stress responses. Altered KY function has been connected to myopathic phenotypes in animal models, making it relevant for studying mechanisms of muscle weakness and degeneration. As a research target, Ky supports investigations into gene networks controlling muscle structure, neuromuscular function, and tissue-specific transcriptional programs.
KY peptidase CRISPR Activation Plasmid (m) provides a targeted, non-destructive approach to upregulating endogenous Ky expression without altering the underlying DNA sequence.
KY peptidase CRISPR Activation Plasmid (m) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the Ky 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 Ky transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous KY peptidase expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native Ky locus and enabling the study of KY peptidase-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of KY peptidase pathway restoration in tumor cells with silenced or reduced Ky expression.
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.