The GALNT7 Knockout Raji Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout cell population generated from the human Raji B lymphocyte line. This product provides targeted disruption of the GALNT7 gene, which encodes polypeptide N-acetylgalactosaminyltransferase 7, the enzyme responsible for initiating mucin-type O-linked glycosylation. The polyclonal nature preserves a mixture of edited alleles without single-cell cloning, offering a heterogeneous population for studying gene function under more physiologically relevant conditions than clonal isolates.
Raji is a well-characterized Burkitt’s lymphoma-derived B cell line that retains key features of mature B lymphocytes, including surface immunoglobulin expression and the ability to secrete antibodies. It is widely employed to investigate B lymphocyte biology, Epstein-Barr virus latency, and oncogenic mechanisms. As a model of aggressive lymphoma, Raji cells enable dissection of signaling pathways governing proliferation, apoptosis, and tumor?Cimmune interactions, providing a relevant backdrop for evaluating glycosylation-related processes.
GALNT7 catalyzes the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc to serine or threonine residues on substrate proteins, initiating O-glycan core synthesis. This modification regulates the stability and function of key glycoproteins, including MUC1, epidermal growth factor receptor (EGFR), and insulin-like growth factor 1 receptor (IGF1R). Transcriptional control by the SP1 factor and growth factor signaling pathways links external cues to glycosylation capacity, thereby modulating receptor activation and downstream signal transduction.
In the Raji B cell context, disruption of GALNT7 eliminates O-glycan initiation on critical substrates, potentially altering EGFR and IGF1R signaling and consequently influencing lymphoma cell survival and proliferation. Altered MUC1 glycosylation may also affect cell adhesion and immune synapse formation, processes frequently dysregulated in hematological malignancies. This knockout model therefore provides a valuable system for interrogating glycosylation-dependent B cell biology and its contribution to lymphoma pathogenesis.
These polyclonal knockout cells are suited for diverse applications, including flow cytometry with glycan-specific probes to assess surface O-glycan changes, western blotting with lectins or anti-glycan antibodies, and co-immunoprecipitation to examine glycosylation-dependent protein complexes. Functional assays such as proliferation, migration, and invasion, combined with RNA-seq-based transcriptomics, can reveal phenotypic consequences. The product additionally serves as a platform for validating glycosyltransferase targets in cancer. For technical inquiries, please contact Ascent Research.
