TINAGL1 CRISPR Activation Plasmid (h): sc-416499-ACT

TINAGL1 (tubulointerstitial nephritis antigen-like 1) encodes a secreted extracellular matrix–associated glycoprotein implicated in cell–matrix adhesion and remodeling of the pericellular environment. It is linked to regulation of cellular behaviors such as migration, adhesion, and survival, processes that intersect with integrin-mediated signaling and extracellular matrix organization. In human tissues and model systems, altered TINAGL1 expression has been associated with changes in epithelial–mesenchymal plasticity and invasive phenotypes, supporting its relevance to studies of tumor progression and metastatic potential. As a matricellular factor, TINAGL1 provides a useful handle for interrogating how extracellular cues shape signaling networks and microenvironment-dependent cell states.

TINAGL1 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous TINAGL1 expression without altering the underlying DNA sequence.

TINAGL1 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the TINAGL1 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 TINAGL1 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous TINAGL1 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native TINAGL1 locus and enabling the study of TINAGL1-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of TINAGL1 pathway restoration in tumor cells with silenced or reduced TINAGL1 expression.

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