Serglycin CRISPR Activation Plasmid (h): sc-404207-ACT

SRGN encodes serglycin, a secreted and granule-resident proteoglycan that carries chondroitin sulfate chains and functions as a scaffold for cationic mediators such as proteases, chemokines, and growth factors. In immune and hematopoietic cells, serglycin supports regulated secretory granule biogenesis, cargo retention, and stimulus-dependent exocytosis, shaping inflammatory signaling, extracellular matrix remodeling, and cell–cell communication. Its activity intersects with degranulation-associated pathways in mast cells, cytotoxic lymphocytes, and myeloid lineages, influencing protease-driven signaling networks and chemokine availability. Dysregulated SRGN expression has been associated with altered immune microenvironments and tumor–stroma interactions, making it relevant for studies of inflammation-linked disease mechanisms and cancer biology.

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

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

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