The FAM98B Knockout Raji Polyclonal Cells are a CRISPR/Cas9-edited polyclonal population derived from the Raji B lymphoblastoid cell line, providing a constitutive loss-of-function model for the FAM98B locus. This gene disruption generates a heterogeneous mix of edited alleles across the cell pool, stably eliminating wild-type protein expression. The polyclonal format avoids the clonal variation and selection bias of monoclonal isolates, yielding a more representative knockout phenotype. Researchers can employ these cells to dissect FAM98B??s role as a structural organizer within the methylosome and its downstream effects on arginine methylation and spliceosomal dynamics. This model is suitable for studies demanding reliable gene inactivation without single-cell cloning.
Raji cells are an EBV-immortalized B lymphocyte line established from a Burkitt lymphoma patient, characterized by high proliferative capacity and expression of mature B cell markers including CD19, CD20, and surface immunoglobulin. This suspension culture model is employed to investigate B cell receptor signaling, oncogenic transformation, and therapeutic sensitivity in lymphoma. The EBV latency III program drives constitutive NF-??B and JAK/STAT activation, creating a pro-survival background mimicking aggressive B cell malignancies. Because Raji cells retain functional methylation and splicing machineries, they provide a relevant host for analyzing FAM98B-dependent methylosome activity in a lymphomagenic context where arginine methylation is often dysregulated.
FAM98B protein is an integral scaffold of the methylosome complex, bridging PRMT5 with its cofactor MEP50/WDR77 to facilitate symmetric dimethylation of specific Sm proteins. This modification on C-terminal arginine residues of SmB/B??, SmD1, and SmD3 is essential for spliceosomal snRNP core particle assembly and pre-mRNA splicing. Within the methylosome, FAM98B directly interacts with PRMT5 and MEP50, positioning Sm substrates for efficient catalysis. Loss of FAM98B disrupts this coordination, causing hypomethylated Sm proteins, defective snRNP maturation, and global splicing perturbations. Consequently, FAM98B acts as a critical regulatory node linking arginine methylation to transcriptome fidelity, with downstream effects on gene expression programs that may influence B cell growth and viability.
Within the Raji Burkitt lymphoma model, FAM98B ablation creates a platform for investigating methylosome-dependent vulnerabilities in B cell cancers. Although not well characterized in lymphoma, arginine methylation pathways are frequently dysregulated in hematologic malignancies, suggesting methylosome integrity may affect malignant phenotypes. By knocking out FAM98B in an EBV-driven, proliferating B cell line, researchers can assess how disruption of Sm protein methylation alters splicing-dependent expression of oncogenes or tumor suppressors. This model may reveal synthetic lethal interactions with methylation inhibitors or spliceosome modulators, aiding identification of therapeutic targets for Burkitt lymphoma and related neoplasms.
The FAM98B Knockout Raji Polyclonal Cells enable western blotting for knockout confirmation and methylation detection, RT-qPCR for expression changes, RNA-seq for splicing analysis, and flow cytometry for B cell surface markers. Proliferation and drug sensitivity assays can test fitness effects. These cells are also suitable for CRISPR modifier screens. For further information, please contact Ascent Research.
