The B4GALT1 Knockout SK-OV-3 Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout cell population in which B4GALT1 gene disruption yields a loss-of-function model. This product consists of a heterogeneous pool of SK-OV-3 human ovarian adenocarcinoma epithelial cells harboring diverse genetic alterations that collectively eliminate functional B4GALT1 protein expression. The polyclonal format avoids clonal selection bias and is well-suited for population-level phenotypic analyses and pooled functional genomics studies.
The parental SK-OV-3 cell line, isolated from the ascites of a 64-year-old female with ovarian adenocarcinoma, is a widely used model for ovarian cancer metastasis and chemoresistance. These cells exhibit epithelial morphology, carry wild-type TP53, and are tumorigenic in immunocompromised mice, recapitulating key features of high-grade serous carcinoma. Their robust growth and well-characterized genomic landscape provide a reliable background for investigating glycogene function in ovarian cancer progression.
B4GALT1 encodes a Golgi-resident ??-1,4-galactosyltransferase that catalyzes the transfer of galactose from UDP-galactose to terminal N-acetylglucosamine residues on nascent glycoproteins and glycolipids, playing a central role in protein N-glycosylation and glycosphingolipid biosynthesis. Transcription of B4GALT1 is positively regulated by SP1 and responsive to TGF-?? signaling, while its enzymatic activity is modulated by interactions with alpha-lactalbumin and the Golgi glycosyltransferase complex. Downstream, B4GALT1-mediated galactosylation modifies key cell surface molecules including integrins, epidermal growth factor receptor (EGFR), and E-cadherin, thereby influencing cell adhesion, migration, and receptor-mediated signaling. Knockout of this gene truncates glycans, leading to an accumulation of exposed N-acetylglucosamine residues and loss of galactose-terminated epitopes recognized by endogenous lectins, with consequences for immune recognition and cellular communication.
In the SK-OV-3 ovarian cancer context, B4GALT1 loss disrupts the glycosylation of adhesion and signaling receptors, attenuating integrin-dependent matrix attachment, EGFR-driven proliferation, and E-cadherin-mediated cell-cell cohesion. These molecular changes are predicted to impair metastatic potential and may alter interactions with the tumor microenvironment, including modulation of natural killer cell and galectin-based immune surveillance. The polyclonal knockout population captures a spectrum of editing outcomes, reflecting the intratumoral heterogeneity of glycosylation patterns observed in clinical ovarian tumors and enabling robust functional evaluation.
This knockout model is suitable for a range of experimental approaches, including lectin blotting with RCA-I and flow cytometry using galactose-specific lectins to confirm alteration of glycoprofiles, as well as transwell migration and invasion assays to assess metastatic behavior. It can be utilized for mass spectrometry-based glycomic analysis and western blot detection of glycoproteins such as integrins and EGFR. Further applications encompass screening of therapeutics that target the glycocalyx and investigating tumor-immune cell interactions. For additional information or technical support, please contact Ascent Research.
