Myosin VIIB CRISPR Activation Plasmid (h): sc-409183-ACT

Human MYO7B encodes Myosin VIIB, an actin-based motor protein that supports cytoskeletal organization and intracellular transport processes linked to cell polarity and specialized membrane domain maintenance. As a member of the unconventional myosin family, it is implicated in actin filament dynamics, vesicle trafficking, and scaffolded signaling events that shape epithelial architecture. Dysregulation of actin-dependent transport and polarity pathways is frequently studied in contexts such as barrier function defects and altered tissue organization relevant to gastrointestinal and sensory systems. MYO7B modulation is therefore useful for dissecting how actin motors coordinate trafficking, adhesion complexes, and junctional remodeling in human cells.

Myosin VIIB CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous MYO7B expression without altering the underlying DNA sequence.

Myosin VIIB CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the MYO7B 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 MYO7B transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous Myosin VIIB expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native MYO7B locus and enabling the study of Myosin VIIB-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of Myosin VIIB pathway restoration in tumor cells with silenced or reduced MYO7B expression.

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