The B3GALNT2 Knockout A-549 Polyclonal Cells product provides a CRISPR/Cas9-edited polyclonal knockout cell population derived from human A-549 lung adenocarcinoma cells, featuring targeted disruption of the B3GALNT2 gene. This pool of gene-edited cells serves as a consistent loss-of-function model to investigate O-mannose glycosylation pathways and dystroglycan biology in a cancer-relevant setting. The polyclonal nature captures a spectrum of editing events, offering a heterogeneous cell population that reflects genetic diversity without requiring clonal isolation. Researchers can employ this tool to dissect glycosylation-dependent adhesion, signaling, and disease mechanisms.
The host A-549 cell line is a widely used epithelial model originating from human lung adenocarcinoma, retaining characteristics of alveolar type II pneumocytes. It is extensively applied in cancer biology, respiratory research, and drug screening, expressing key glycoproteins and adhesion molecules. This background provides a physiologically pertinent context for studying how altered glycosylation influences tumor cell behavior, including adhesion, migration, and response to therapeutic agents.
B3GALNT2 encodes a Golgi-resident glycosyltransferase that catalyzes the addition of N-acetylgalactosamine (GalNAc) via ??1,3-linkage to O-mannose residues on ??-dystroglycan (DAG1). This step is required for LARGE and B4GAT1 to subsequently build the functional laminin-binding glycan. B3GALNT2 forms complexes with LARGE, B4GAT1, and other Golgi glycosyltransferases. The pathway is regulated by cell-specific transcription factors and possibly the unfolded protein response; disruption impairs DAG1 interactions with laminin, causing defective adhesion and signaling.
In the A-549 adenocarcinoma context, B3GALNT2 knockout impairs dystroglycan glycosylation, compromising laminin binding and altering cell spreading and motility. This enables direct investigation of dystroglycanopathies at the cellular level and also sheds light on the role of glycosylation in lung cancer progression, including invasion and metastasis. The polyclonal knockout pool provides a robust, population-based model for studying how loss of this glycosyltransferase affects cancer cell behavior and microenvironment interactions.
This cell product supports a wide array of experimental applications. Western blotting with IIH6 antibody, lectin blotting, and immunofluorescence microscopy enable assessment of dystroglycan glycosylation status. Cell adhesion assays on laminin quantify functional consequences, while flow cytometry and mass spectrometry allow profiling of cell-surface glycans. Functional migration and invasion assays can be combined with drug sensitivity testing for screening glycosylation-targeted therapies. This model is also valuable for mechanistic studies in congenital disorders of glycosylation and for exploring glycobiology in other cellular processes. For more details, please contact Ascent Research.
