The B4GALT1 Knockout UM-UC-3 Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout cell population derived from the UM-UC-3 human bladder carcinoma cell line, designed for loss-of-function studies of the B4GALT1 gene. This polyclonal pool contains a heterogeneous mixture of cells harboring diverse disruptions at the B4GALT1 locus, ensuring representation of various editing events without clonal bias. The knockout abolishes expression of ??-1,4-galactosyltransferase 1, a key enzyme in glycoconjugate biosynthesis, providing a versatile model to interrogate glycosylation-dependent processes in cancer biology.
The parental UM-UC-3 cell line originates from a male patient with transitional cell carcinoma of the urinary bladder and is widely established as a model for urothelial carcinoma research. These cells exhibit epithelial morphology, retain tumorigenic capacity in immunodeficient mice, and represent a well-characterized system for investigating molecular mechanisms underlying bladder cancer progression. Their robust in vitro growth and experimental tractability make them a valuable host for genetic perturbation studies, particularly for exploring the role of glycosyltransferases in tumor cell behavior.
B4GALT1 encodes ??-1,4-galactosyltransferase 1, which catalyzes the transfer of galactose from UDP-galactose to N-acetylglucosamine residues on glycoproteins and glycolipids. This enzymatic activity is central to N-glycan and glycosphingolipid biosynthesis, modulating cell adhesion through laminin binding and downstream signaling. B4GALT1 is transcriptionally regulated by TGF-??1, EGF, IL-6, and NF-??B via SP1 and STAT3, and its product influences integrin ??1 galactosylation, FAK phosphorylation, and ERK activation. Additionally, B4GALT1 interacts with ??-lactalbumin to form the lactose synthase complex and associates with caveolin-1 and integrin subunits ITGA6 and ITGB1, linking glycosylation to ECM-receptor interaction and immune modulation.
In the context of UM-UC-3 bladder cancer cells, knockout of B4GALT1 disrupts the normal glycosylation landscape, impairs laminin-mediated cell adhesion, and attenuates integrin-driven signaling cascades. This molecular perturbation is expected to alter tumor cell migration, invasion, and potentially immune recognition, reflecting the importance of cell surface glycan structures in malignant progression. The UM-UC-3 background provides a clinically relevant platform for dissecting how glycosylation defects contribute to bladder cancer pathology, including potential links to congenital disorders of glycosylation type IId.
This polyclonal knockout product is suited for a range of investigative applications, including functional genomics studies of B4GALT1 in bladder cancer progression, interrogation of glycosylation-dependent cell adhesion and motility using transwell migration and laminin adhesion assays, and validation of glycosylation inhibitors as therapeutic candidates. Additional uses encompass phospho-signaling analysis of FAK and ERK pathways, lectin blotting with RCA-I to assess galactosylation status, and glycan profiling by mass spectrometry. The cells also support RT-qPCR screening of glycosylation-related gene expression changes and flow cytometric evaluation of cell surface glycans. For further technical details or customization options, please contact Ascent Research.
