The C1GALT1 Knockout HT29 Polyclonal Cells product is a CRISPR/Cas9-edited polyclonal knockout cell population derived from the human HT29 colorectal adenocarcinoma cell line. This product delivers targeted disruption of the C1GALT1 gene in a genetically heterogeneous pool, providing a robust loss-of-function model for core 1 synthase studies. The polyclonal format maintains biological variability and is ideal for pooled assays in glycobiology and cancer research.
The HT29 cell line is a well-established model of human intestinal epithelial biology, originating from a colorectal adenocarcinoma. These epithelial cells express mucins and retain characteristics of absorptive and mucus-secreting intestinal cells, making them broadly used in colorectal cancer, mucosal immunology, and epithelial barrier research. HT29 cells provide a physiologically relevant context for investigating O-glycosylation pathways and their implications in tumor progression and inflammatory bowel disease.
The C1GALT1 gene encodes the core 1 ??1,3-galactosyltransferase, which catalyzes the addition of galactose to O-linked N-acetylgalactosamine to form core 1 O-glycans on mucins and glycoproteins. Its expression is transcriptionally regulated by SP1 and NF-??B and is induced downstream of TGF?? signaling. The enzyme requires the COSMC molecular chaperone for proper folding and stability. Core 1 O-glycans on substrates such as MUC1, MUC2, and CD43 critically modulate integrin signaling and cell adhesion molecule function.
Disruption of C1GALT1 in HT29 cells abolishes core 1 O-glycan synthesis, leading to surface expression of truncated Tn antigen on mucins like MUC1 and MUC2. This glycan truncation compromises the mucus barrier and perturbs cell adhesion, migration, and immune recognition, recapitulating features of colorectal cancer where Tn antigen correlates with metastasis and poor prognosis. The knockout model also facilitates investigation of glycosylation-driven epithelial changes in inflammatory bowel disease.
These polyclonal knockout cells are a versatile platform for studying O-glycosylation in cancer, Tn antigen biology, and glycan-mediated immune evasion. Researchers can utilize lectin blotting with PNA and VVA, flow cytometry for Tn antigen, western blotting for C1GALT1, and MUC1 O-glycosylation analysis. Functional assays such as cell adhesion, migration, and proliferation enable dissection of glycan-dependent behaviors. The product supports drug screening targeting glycosylation pathways and mechanistic mucin research. For additional information or technical support, please contact Ascent Research.
