The EIF4G3 Knockout Raji Polyclonal Cells product offers a CRISPR/Cas9-edited polyclonal knockout cell population derived from the human Raji B lymphoblastoid cell line. This loss-of-function model features targeted disruption of the EIF4G3 gene, which encodes a critical scaffolding component of the eukaryotic translation initiation factor 4F (eIF4F) complex. The polyclonal nature of the knockout population ensures representation of diverse editing events across the cell pool, providing a robust tool for studying gene function without clonal selection artifacts. This product is designed for researchers investigating cap-dependent translation mechanisms, signal transduction pathways regulating protein synthesis, and translational dysregulation in B-cell malignancies.
The Raji host cell line, derived from an EBV-positive Burkitt’s lymphoma patient, is a suspension-adapted B lymphoblastoid cell line widely employed in immunology and oncology research. These cells actively produce antibodies and function in antigen presentation, mirroring key aspects of B-cell biology. The EBV positivity and lymphoblastoid phenotype make Raji cells a relevant model for studying lymphomagenesis, viral interactions, and translational control in transformed B cells. Their suspension growth facilitates scalable culture and a variety of biochemical assays, including those that require large cell numbers for polysome fractionation or immunoprecipitation.
EIF4G3 functions as a central scaffold within the eIF4F translation initiation complex, bridging the mRNA 5′ cap-binding protein eIF4E and the 3′ poly(A)-binding protein PABPC1 to circularize mRNA, a configuration that enhances ribosome recycling and translation efficiency. It also recruits the eIF4A RNA helicase to unwind secondary structures in 5′ untranslated regions (UTRs), facilitating 40S ribosomal subunit scanning. EIF4G3 activity is regulated by upstream signaling modules, including mTOR kinase and the MAPK/ERK pathway, which converge on eIF4E phosphorylation via MNK kinases. Upon activation, EIF4G3 promotes global cap-dependent translation, but it is particularly critical for mRNAs harboring structured 5′ UTRs, such as those encoding MYC, BCL2, and CCND1. The eIF4F complex also interacts with eIF3 to recruit the 40S ribosome. Together, these molecular interactions place EIF4G3 at a nodal point linking mitogenic and nutrient signaling to the translational machinery.
In the Raji B-cell lymphoma context, EIF4G3 disruption provides a powerful avenue to dissect the role of translation initiation in lymphomagenesis. Many B-cell malignancies, including Burkitt’s lymphoma, exhibit elevated eIF4F activity driven by oncogenic signaling, leading to selective translation of pro-growth and anti-apoptotic mRNAs. Knocking out EIF4G3 in Raji cells allows researchers to interrogate how loss of scaffold function impacts the translation of key lymphomagenic drivers like MYC and BCL2. Moreover, Raji cells’ EBV positivity raises questions about viral mRNA translation, which often relies on host eIF4F components; thus, the knockout model can be applied to study herpesviral mRNA utilization. The model also supports investigations into how altered translation affects antibody production and antigen presentation in B-cell lines.
Researchers can employ the EIF4G3 Knockout Raji Polyclonal Cells in a wide array of functional assays. Polysome profiling and ribosome footprinting enable direct assessment of global and mRNA-specific translation changes, while luciferase reporter constructs driven by cap-dependent elements quantify initiation efficiency. Western blotting for eIF4F components (eIF4E, eIF4A, PABPC1) reveals complex integrity, and m7GTP pull-down assays or RNA immunoprecipitation (RIP) can measure cap-binding activity and mRNA association. Cell proliferation assays provide insights into the phenotypic consequences of translation dysregulation. These applications are particularly relevant for drug discovery programs targeting translation, including compounds aimed at eIF4E/eIF4G interactions or upstream kinases. For additional information or to request a quotation, please contact Ascent Research.
