golgin 97 CRISPR Activation Plasmid (h): sc-403152-ACT

GOLGA1 encodes golgin 97, a coiled-coil peripheral membrane protein enriched at the trans-Golgi network that helps maintain Golgi architecture and supports vesicle tethering during post-Golgi trafficking. By coordinating cargo sorting and retrograde transport pathways between the Golgi, endosomes, and plasma membrane, golgin 97 contributes to membrane homeostasis and the fidelity of secretory pathway organization. Perturbation of Golgi tethering and trafficking factors is linked to altered receptor recycling, stress responses, and mislocalization of glycosylation enzymes, processes frequently examined in neurodegeneration, infection biology, and cancer cell phenotypes. As a marker and regulator of TGN dynamics, golgin 97 is commonly studied in assays of organelle structure, vesicular transport kinetics, and proteostasis under cellular stress.

golgin 97 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous GOLGA1 expression without altering the underlying DNA sequence.

golgin 97 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the GOLGA1 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 GOLGA1 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous golgin 97 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native GOLGA1 locus and enabling the study of golgin 97-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of golgin 97 pathway restoration in tumor cells with silenced or reduced GOLGA1 expression.

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