UGTREL1 CRISPR Activation Plasmid (h): sc-411438-ACT

SLC35B1 encodes the human nucleotide-sugar transporter UGTREL1, a multi-pass membrane protein that supports glycosylation by supplying activated sugars to the luminal side of the endoplasmic reticulum and/or Golgi apparatus. By regulating substrate availability for glycosyltransferases, UGTREL1 influences protein N-linked glycosylation, quality control, and trafficking, with downstream effects on receptor maturation and secretory pathway homeostasis. Perturbation of nucleotide-sugar transport can remodel cell-surface glycans and alter signaling, adhesion, and stress responses, making SLC35B1 relevant to studies of glycoproteostasis and pathway rewiring in disease-associated cellular states. As a result, SLC35B1 is frequently investigated in the context of metabolic–secretory coupling, organelle function, and glycan-dependent regulation of immune and growth-factor pathways.

UGTREL1 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous SLC35B1 expression without altering the underlying DNA sequence.

UGTREL1 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the SLC35B1 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 SLC35B1 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous UGTREL1 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native SLC35B1 locus and enabling the study of UGTREL1-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of UGTREL1 pathway restoration in tumor cells with silenced or reduced SLC35B1 expression.

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