The B3GNT4 Knockout HEK293T Polyclonal Cells represent a CRISPR/Cas9-edited polyclonal knockout cell population derived from HEK293T cells, targeting the human B3GNT4 gene encoding a key glycosyltransferase involved in poly-N-acetyllactosamine (poly-LacNAc) biosynthesis. This gene-edited model offers a robust loss-of-function research tool for investigating B3GNT4-dependent glycosylation processes and their functional consequences.
HEK293T is a widely utilized human embryonic kidney epithelial cell line that stably expresses the SV40 large T-antigen, enabling episomal replication of transfected plasmids and high-level protein expression. Its epithelial origin and robust growth characteristics make it a standard model for studying signaling pathways, viral production, and recombinant protein expression in biomedical research.
B3GNT4 catalyzes the elongation of poly-LacNAc chains on glycoproteins, a critical modification that regulates cell surface receptor function. Transcriptionally regulated by SP1 and TGF-beta signaling, B3GNT4 acts within the Golgi apparatus, often in concert with other glycosyltransferases such as B3GNT2 and galactosyltransferases. Downstream, B3GNT4-mediated glycosylation modulates integrin activity and focal adhesion kinase (FAK) signaling, thereby influencing the PI3K-AKT pathway and cell migration effectors. Disruption of B3GNT4 is expected to alter N-glycan processing and cell adhesion signaling networks.
In HEK293T cells, knockout of B3GNT4 abolishes poly-LacNAc chain elongation on glycoproteins, leading to potential changes in integrin glycosylation and downstream focal adhesion dynamics. This makes the polyclonal knockout population a physiologically relevant model for dissecting glycosylation-dependent cell adhesion, migration, and signal transduction in a human epithelial context, with implications for understanding cancer metastasis and glycopathology.
These polyclonal knockout cells are suitable for a wide range of experimental applications, including lectin-based glycosylation profiling, Western blotting to assess glycoprotein alterations, transwell migration and wound healing assays to evaluate cell motility, immunofluorescence for focal adhesion architecture, and flow cytometry for cell surface glycan analysis. The model supports drug target validation and cancer cell biology studies focused on glycosyltransferase function. For more information, please contact Ascent Research.
