Genome-edited Cells
Lung
The GALNT14 Knockout NCI-H520 Cell Line offers a CRISPR/Cas9-mediated knockout of GALNT14 in the human lung squamous carcinoma cell line NCI-H520. GALNT14 initiates mucin-type O-glycosylation by transferring GalNAc to protein substrates, impacting cancer-related processes such as cell adhesion and signaling. This model provides a defined system to study O-glycosylation in lung cancer progression and metastasis. Key molecular partners include the upstream transcription factor SP1, the downstream targets MUC1 and MUC16, and the glycosyltransferases C1GALT1 and ST3GAL1. Applications encompass western blotting for glycoprotein changes, lectin-based glycan profiling, and functional assays for migration and invasion, facilitating detailed dissection of glycosylation-driven tumor phenotypes.
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The GALNT14 Knockout NCI-H520 Cell Line is a CRISPR/Cas9-edited knockout cell line derived from human lung squamous cell carcinoma NCI-H520 cells. This cell line carries a targeted disruption of GALNT14, the gene encoding polypeptide N-acetylgalactosaminyltransferase 14, which initiates O-linked glycosylation. As a loss-of-function model, it enables investigation of GALNT14-mediated glycosylation in cancer. CRISPR/Cas9-mediated gene disruption generates a stable knockout without specifying clonality. This tool is designed for advanced biomedical research.
NCI-H520 is an epithelial cell line derived from human lung squamous cell carcinoma, a major form of non-small cell lung cancer. These malignant squamous epithelial cells are widely used to study lung cancer pathogenesis, tumor progression, and drug responses. The parental line preserves O-glycosylation machinery, providing a suitable background to perturb GALNT14 and assess its contributions to glycoprotein alterations in a cancerous setting. Introducing a knockout in these cells enables direct functional analyses in a disease-relevant model.
GALNT14 catalyzes the transfer of N-acetylgalactosamine (GalNAc) to serine/threonine residues, the initial step of mucin-type O-glycosylation, requiring Mn2+ as a cofactor. The enzyme interacts with acceptor substrates and other glycosyltransferases including C1GALT1 and ST3GAL1 for glycan elongation. Upstream, SP1 transcriptionally regulates GALNT14 downstream of cancer pathways. Key downstream targets are mucins MUC1 and MUC16 and cell adhesion molecules; their glycosylation affects stability, cell?Ccell interactions, and signaling. Through these interactions, GALNT14 modulates cell adhesion, migration, and invasion??processes often altered in cancer.
In NCI-H520 lung squamous carcinoma cells, GALNT14 knockout serves as a model to study how loss of O-glycosylation initiation influences tumor cell behavior. Because GALNT14 glycosylates mucins and adhesion proteins that shape cell surface properties and signaling, its disruption likely alters pathways driving metastasis and progression. This cell line enables dissection of GALNT14-dependent malignancy features, including aberrant migration, invasion, and potential immune evasion. It also facilitates exploration of crosstalk between O-glycosylation and SP1-mediated oncogenic signaling.
The GALNT14 Knockout NCI-H520 Cell Line supports functional assays such as western blotting with glycoprotein-specific probes, lectin-based glycan profiling, and cell migration/invasion assays to evaluate metastatic behavior. It is suitable for complementation experiments, drug screens targeting glycosylation, and signaling studies downstream of mucins. By offering a defined genetic background, this model advances rigorous investigation of GALNT14 function in lung cancer and O-glycobiology. For more information or to inquire about this product, please contact Ascent Research.
