The FGB Knockout Raji Polyclonal Cells represent a CRISPR/Cas9-edited polyclonal knockout cell population derived from the Raji B lymphocyte cell line, engineered to carry a targeted disruption of the FGB gene. This polyclonal format provides a heterogeneous pool of edited cells, offering a robust model for studying fibrinogen beta chain function without clonal selection bias. The CRISPR/Cas9-mediated gene disruption abrogates FGB expression, enabling loss-of-function analyses in a well-characterized human B-cell background. These cells are supplied as a ready-to-use knockout population suitable for a range of downstream functional assays.
The parental Raji cell line is an Epstein-Barr virus (EBV)-positive human B lymphocyte line originally established from a Burkitt’s lymphoma patient. As a model for B-cell malignancies, Raji cells exhibit characteristics of germinal center B cells and are widely employed in hematological cancer research to investigate immune signaling, apoptosis regulation, and tumor microenvironment interactions. Their robust proliferation and well-documented molecular profile make them an ideal host for gene knockout studies aimed at dissecting pathways relevant to lymphomagenesis and B-cell biology.
FGB encodes the fibrinogen beta chain, an essential subunit of the fibrinogen glycoprotein that is proteolytically activated by thrombin to form fibrin during coagulation. Beyond its canonical role in hemostasis, fibrin(ogen) engages integrin receptors such as ??IIb??3 on platelets and ??M??2 (Mac-1) on leukocytes, mediating platelet aggregation, leukocyte adhesion, and transendothelial migration. Fibrinogen expression is transcriptionally regulated by IL-6, oncostatin M, glucocorticoids, and TGF-?? via STAT3 and C/EBP??, while downstream effectors include VE-cadherin-dependent endothelial adhesion, plasmin-mediated fibrinolysis, and pro-inflammatory cytokine release. Interaction partners like factor XIIIa, fibronectin, and VEGF further integrate fibrinogen into wound healing and angiogenic processes.
In the Raji B-cell context, FGB knockout provides a unique tool to investigate coagulation-independent functions of fibrinogen in lymphocyte biology and tumor pathogenesis. While fibrinogen is primarily hepatic, its expression in leukocytes and its ability to modulate integrin-dependent adhesion and inflammatory signaling may influence lymphoma cell interactions with the microenvironment. By eliminating FGB in these cells, researchers can explore how the fibrinogen beta chain affects B-cell receptor signaling, cytokine networks, and extracellular matrix adhesion, potentially revealing novel roles in immune surveillance evasion and metastatic behavior.
This polyclonal knockout model is applicable to diverse experimental workflows including Western blotting and RT-qPCR for expression analysis, fibrinogen ELISA for secreted protein quantification, and cell adhesion assays to assess integrin-dependent binding to endothelial cells or matrix components. Co-culture systems with platelets permit evaluation of fibrinogen??s contribution to tumor cell?Cplatelet aggregates, while migration and invasion assays can elucidate its role in lymphoma dissemination. Flow cytometry of integrin ??M??2 or ??IIb??3, cytokine profiling, and RNA-seq transcriptional analysis provide further mechanistic resolution. For detailed protocols or further technical consultation, please contact Ascent Research.
