The B4GALT1 Knockout HCT 116 Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout cell population derived from the human colorectal carcinoma HCT 116 cell line, featuring targeted disruption of the B4GALT1 gene. This polyclonal knockout pool provides a versatile loss-of-function model for investigating the roles of beta-1,4-galactosyltransferase in glycoprotein and glycolipid biosynthesis, without claims of clonality or specific editing outcomes. The heterogeneous population retains genetic diversity, making it suitable for functional studies that require a representative knockout background in colorectal cancer research.
HCT 116 is a widely characterized human colorectal carcinoma epithelial cell line isolated from a male patient with colorectal carcinoma. It serves as a robust model for intestinal epithelial cancer, commonly employed to study molecular mechanisms underlying colorectal carcinogenesis, metastasis, and therapeutic responses. This adherent cell line harbors mutations relevant to cancer signaling and provides a physiologically relevant host background for examining glycosylation alterations in colorectal cancer, inflammatory bowel disease, and congenital disorders of glycosylation.
B4GALT1 encodes beta-1,4-galactosyltransferase, which catalyzes the transfer of galactose from UDP-galactose to N-acetylglucosamine to form the Gal??1-4GlcNAc (lactosamine) linkage on N- and O-glycans and glycosphingolipids. This reaction is central to the biosynthesis of complex glycoconjugates and is regulated by transcription factors SP1 and NF-??B, along with signaling pathways mediated by EGFR and TGF-??. The enzyme interacts with alpha-lactalbumin and the oligosaccharyltransferase complex, and its activity influences downstream glycosylation of integrins, cadherins, and growth factor receptors, thereby modulating cell adhesion, migration, and intracellular signaling cascades.
In HCT 116 colorectal carcinoma cells, disruption of B4GALT1 alters glycosylation patterns critical for tumor cell behavior. Aberrant glycosylation of integrins and cadherins can impair cell-cell and cell-matrix adhesion, potentially influencing metastasis. Additionally, altered glycosylation of receptors such as EGFR may affect downstream signaling pathways, including those regulated by EGFR and TGF-??. This knockout model thus provides a physiologically relevant setting to dissect how changes in galactosyltransferase activity contribute to colorectal cancer progression, inflammatory bowel disease, and congenital disorders of glycosylation type IId (CDG-IId).
These polyclonal knockout cells are ideal for a range of functional assays, including western blotting with lectins to assess global glycosylation changes, flow cytometry for cell surface glycan profiling, cell adhesion and migration/invasion assays to evaluate metastatic potential, RT-qPCR to quantify glycosylation-related gene expression, and mass spectrometry-based glycomics for detailed glycan structural analysis. They can be applied to investigate glycosylation??s role in cancer progression, model CDG-IId, study immune recognition through glycans, and screen compounds targeting glycosylation pathways. For further information on employing this B4GALT1 knockout model in your research, please contact Ascent Research.
