The FBXO25 Knockout Raji Polyclonal Cells are a CRISPR/Cas9-mediated gene-disrupted cell pool derived from the Raji B-cell line. This polyclonal product offers a heterogeneous knockout population in which FBXO25 gene function is broadly abrogated, facilitating loss-of-function studies without the constraints of monoclonal selection. The targeted disruption of FBXO25 eliminates the substrate-recognition subunit of the SCF E3 ubiquitin ligase complex, providing a direct tool to query FBXO25-dependent processes in a disease-relevant B-lymphocyte background.
The parental Raji cell line, an EBV-positive Burkitt lymphoma model, is widely employed to dissect B-cell biology and oncogenic signaling. Derived from a Burkitt lymphoma patient, these suspension-adapted B lymphocytes retain characteristic NF-??B activation and apoptotic pathways that intersect with ubiquitin-proteasome regulation. The EBV-driven background further mimics viral latency and immune evasion mechanisms, making Raji cells an ideal host for investigating the crosstalk between viral infection, NF-??B signaling, and proteostatic control.
FBXO25 acts as the substrate-recognition component of the SCF E3 ubiquitin ligase, assembling with SKP1, CUL1, and RBX1 to conjugate ubiquitin onto specific targets. It directly engages HAX-1 and ELF4, promoting their proteasomal clearance. This ubiquitin-dependent degradation regulates apoptotic sensitivity and antiviral innate immune signaling. Transcriptional control upstream of FBXO25 involves NF-??B and stress-responsive pathways, while downstream, loss of HAX-1 triggers apoptosis and ELF4 degradation dampens interferon production. Consequently, FBXO25 coordinates proteostasis with cell death and immune defense mechanisms.
In Raji B lymphocytes, the FBXO25 knockout disrupts a key regulatory intersection between ubiquitin-mediated proteolysis, NF-??B-driven survival signals, and EBV-associated latency programs. The EBV-positive lymphoma background endows these cells with constitutive NF-??B activity and altered apoptotic thresholds; ablating FBXO25 allows direct interrogation of how the SCF E3 ligase machinery shapes B-cell malignancy phenotypes and antiviral responses. This model is particularly suited for disentangling the FBXO25-dependent control of apoptosis versus innate immunity in a B-cell lymphoma context where viral oncoproteins and host ubiquitin pathways converge.
Researchers can deploy this polyclonal knockout model in a variety of functional assays, including immunoblotting and RT-qPCR to confirm gene disruption, co-immunoprecipitation to map altered protein interactions, and apoptosis or NF-??B luciferase reporter assays to quantify signaling changes. Flow-cytometric phenotyping, phospho-protein profiling, and antiviral response analyses further enable dissection of FBXO25??s role in B-cell signaling and virus-host interactions. These tools facilitate investigations into ubiquitin-dependent degradation in cancer, viral infection, and neurodegenerative disorders, and support drug discovery efforts targeting the SCF E3 ligase pathway. For additional information or technical support, please contact Ascent Research.
