The B4GALT1 Knockout T-47D Polyclonal Cells represent a CRISPR/Cas9-edited polyclonal knockout cell population derived from the T-47D human breast cancer cell line, designed to eliminate functional expression of the B4GALT1 gene. This loss-of-function model is generated through CRISPR/Cas9-mediated gene disruption, resulting in a heterogeneous pool of cells harboring various gene edits that collectively abolish B4GALT1 protein activity.
T-47D is a widely used human mammary epithelial cell line derived from the pleural effusion of a patient with breast ductal carcinoma. It represents the luminal A molecular subtype, characterized by estrogen receptor (ER) positivity, progesterone receptor expression, and hormone-responsive growth. These cells retain epithelial morphology and are a key model for studying hormone-dependent breast cancer biology, including estrogen signaling, endocrine therapy response, and tumor microenvironment interactions.
B4GALT1 encodes beta-1,4-galactosyltransferase 1, a key glycosyltransferase that catalyzes the transfer of galactose from UDP-galactose to N-acetylglucosamine residues on glycoproteins and glycolipids. In the mammary epithelium, B4GALT1 interacts with ??-lactalbumin (LALBA) to form the lactose synthase complex, essential for lactose production. Beyond lactose synthesis, B4GALT1-mediated glycosylation modifies cell surface receptors and adhesion molecules, including integrins, cadherins, and EGFR, thereby influencing cell adhesion, migration, and signal transduction. The enzyme??s expression is regulated by hormonal signals such as prolactin, as well as transcription factors STAT3 and NF-??B, placing B4GALT1 at the intersection of glycosylation, hormone response, and oncogenic signaling.
In the context of T-47D ER-positive breast cancer cells, B4GALT1 knockout disrupts the normal glycosylation landscape, potentially impairing the function of integrins and cadherins critical for cell?Ccell and cell?Cmatrix interactions. This alteration may attenuate adhesion-dependent signaling and reduce the metastatic potential of these hormone-responsive cancer cells. Furthermore, loss of B4GALT1-mediated glycosylation of EGFR could affect growth factor receptor trafficking and downstream kinase activation, providing a unique tool to dissect how glycosylation defects intersect with endocrine signaling and tumor progression in a luminal A breast cancer background.
The B4GALT1 Knockout T-47D Polyclonal Cells are suitable for a range of glycobiology and cancer research applications. Researchers can employ lectin blotting or flow cytometry with lectin conjugates to assess global changes in cell surface glycan profiles. Functional consequences can be evaluated using cell adhesion assays on extracellular matrix substrates and migration or invasion assays in Boyden chambers. This model also facilitates investigation of the crosstalk between glycosylation and hormone signaling pathways via RNA-seq or western blotting for key glycoprotein targets such as integrins and EGFR. For additional information or technical support, please contact Ascent Research.
