The GALNT6 Knockout Raji Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout cell population derived from the human Burkitt lymphoma Raji B-cell line, designed to disrupt the GALNT6 gene. This polyclonal model provides a heterogeneous pool of cells carrying GALNT6 loss-of-function mutations, enabling robust functional studies of mucin-type O-glycosylation in a B-lymphocyte context. The product is supplied as a viable polyclonal population, ready for expansion and downstream assays, and is suitable for investigating glycosylation-dependent processes in lymphomagenesis and immune cell biology.
The host Raji cell line is an Epstein-Barr virus (EBV)-positive, immortalized B lymphocyte originally derived from a Burkitt lymphoma patient. Raji cells are widely used as a model for B-cell receptor signaling, apoptosis, and viral oncogenesis due to their stable growth characteristics and retention of key B-cell features. Their transformed phenotype provides a relevant background for examining how altered glycosylation contributes to B-cell malignancies and the interplay between EBV-driven pathways and host cell modifications.
GALNT6 encodes a member of the N-acetylgalactosaminyltransferase family that initiates mucin-type O-glycosylation by transferring GalNAc to serine/threonine residues on target proteins. Key substrates include MUC1, MUC4, the epidermal growth factor receptor (EGFR), and ??1 integrin, whose O-glycosylation status influences protein stability, receptor activation, and cell adhesion. GALNT6 expression is regulated by upstream factors such as SP1, EGF, and TGF-?? signaling, and it functions in concert with C1GALT1 and its chaperone COSMC to extend core 1 O-glycans, thereby modulating pathways including Wnt and integrin signaling.
Disruption of GALNT6 in Raji B cells is expected to impair O-glycosylation of mucins and integrins, leading to altered cell adhesion, migration, and receptor signaling. These changes can affect B-cell interaction with the microenvironment, antigen presentation, and immune recognition, providing a functional link between glycosylation and lymphomagenesis. The knockout model thus offers a relevant system to dissect how aberrant O-glycosylation contributes to B-cell lymphoma progression and potential therapeutic resistance.
Research applications include western blotting and flow cytometry with lectin staining (e.g., Vicia villosa agglutinin) to assess O-glycan profiles, cell adhesion and migration assays, and co-immunoprecipitation to identify GALNT6 substrates. The polyclonal nature supports pooled functional screens and drug sensitivity testing with glycosylation inhibitors, while RNA-seq can reveal global glycosylation gene expression changes. This product is a valuable tool for investigating O-glycosylation in B-cell lymphoma, biomarker discovery, and targeting glycosylation pathways for therapy. For further information or custom requests, please contact Ascent Research.
