Sialyltransferase 7A CRISPR Activation Plasmid (h): sc-406723-ACT

ST6GALNAC1 encodes human Sialyltransferase 7A, a Golgi-resident glycosyltransferase that catalyzes α2,6-sialylation of GalNAc residues on O-glycans, helping shape mucin-type glycosylation patterns at the cell surface and in secreted proteins. By controlling terminal sialic acid display, it influences glycan-dependent processes including protein stability, receptor–ligand interactions, and lectin-mediated signaling within the secretory pathway. Altered ST6GALNAC1 activity can shift sialylated glycoepitope composition and has been linked to changes in cell adhesion and immune recognition contexts, making it relevant to studies of tumor-associated glycosylation and inflammatory microenvironments. This gene is therefore frequently examined in pathway-level analyses of glycosylation remodeling, epithelial differentiation, and cell–matrix communication.

Sialyltransferase 7A CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous ST6GALNAC1 expression without altering the underlying DNA sequence.

Sialyltransferase 7A CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the ST6GALNAC1 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 ST6GALNAC1 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous Sialyltransferase 7A expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native ST6GALNAC1 locus and enabling the study of Sialyltransferase 7A-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of Sialyltransferase 7A pathway restoration in tumor cells with silenced or reduced ST6GALNAC1 expression.

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