The B4GALT1 Knockout MCF-7 Polyclonal Cells product comprises a population of CRISPR/Cas9-edited MCF-7 cells with targeted disruption of the B4GALT1 gene, which encodes beta-1,4-galactosyltransferase 1. This knockout model is provided as a polyclonal cell pool, reflecting a heterogeneous mixture of edited alleles across the population rather than a clonally derived line. The gene disruption is achieved through CRISPR/Cas9-mediated genome editing, resulting in a loss-of-function model suitable for investigating the role of B4GALT1-dependent glycosylation in breast cancer biology.
The host cell line, MCF-7, is a well-characterized human epithelial cell line derived from the pleural effusion of a patient with metastatic breast adenocarcinoma. MCF-7 cells belong to the luminal A molecular subtype, expressing estrogen receptor (ER) and progesterone receptor (PR) while lacking HER2 overexpression, and are widely used as a model for hormone-responsive breast cancer. Their adherent, epithelial morphology and retained hormone signaling pathways make them particularly relevant for studying glycosylation-dependent processes in the context of endocrine-sensitive tumor biology.
B4GALT1 functions as a Golgi-resident glycosyltransferase that catalyzes the transfer of galactose from UDP-galactose to terminal N-acetylglucosamine residues on glycoproteins and glycolipids, generating the Gal??1-4GlcNAc linkage. This enzymatic activity is central to the synthesis of complex N-glycans, O-glycans, and glycosaminoglycan metabolism, as well as to lactose synthesis when complexed with ??-lactalbumin in the mammary gland. Upstream regulation of B4GALT1 is mediated by prolactin-driven STAT5 signaling and by estrogen receptor pathways, while its catalytic products directly modify downstream targets including integrins, the epidermal growth factor receptor (EGFR), and other cell surface receptors, thereby influencing glycoprotein folding, stability, and function. These glycosylation events are critical for cell adhesion, immune recognition, and signal transduction.
In the MCF-7 cellular context, disruption of B4GALT1 ablates a key step in glycoconjugate maturation, potentially altering the glycosylation profile of adhesion molecules and growth factor receptors. This perturbation is expected to impact cell?Ccell and cell?Cmatrix interactions, as well as signaling cascades downstream of EGFR and integrins, which are implicated in the migratory and invasive properties of breast cancer cells. Consequently, the knockout model provides a defined system to dissect the contribution of B4GALT1 to the metastatic phenotype and to explore how aberrant glycosylation intersects with estrogen receptor signaling in breast adenocarcinoma progression.
Researchers can employ this polyclonal knockout population in a variety of experimental settings, including functional glycomics, breast cancer metastasis research, and glycoprotein biosynthesis studies. Representative assays encompass lectin blotting to detect global changes in glycan structures, flow cytometry with glycan-specific probes to profile surface glycosylation, western blotting for target glycoprotein expression, and cell-based assays measuring adhesion, migration, invasion, and proliferation. Glycosyltransferase activity assays can further quantify enzymatic function. For additional technical specifications or lot-specific details, please contact Ascent Research at your convenience.
