CD92 CRISPR Activation Plasmid (h): sc-408392-ACT

SLC44A1 encodes CD92, a choline transporter-like membrane protein that contributes to cellular choline uptake and phospholipid metabolism, supporting membrane biogenesis and signaling demands in proliferating cells. By influencing choline availability, CD92 is linked to pathways governing phosphatidylcholine synthesis, organelle membrane homeostasis, and broader lipid-associated stress responses. Altered expression or regulation of choline transport components has been associated with metabolic remodeling observed in cancer biology and with perturbations in neuroimmune and inflammatory contexts, making SLC44A1 a useful node for mechanistic studies of membrane lipid metabolism. CD92 localization and transport activity also provide a tractable readout for interrogating how nutrient transport interfaces with cell growth and differentiation programs.

CD92 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous SLC44A1 expression without altering the underlying DNA sequence.

CD92 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the SLC44A1 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 SLC44A1 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous CD92 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native SLC44A1 locus and enabling the study of CD92-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of CD92 pathway restoration in tumor cells with silenced or reduced SLC44A1 expression.

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