The PAFAH1B3 Knockout Raji Polyclonal Cells represent a CRISPR/Cas9-edited polyclonal knockout cell population derived from the Raji B lymphocyte cell line. This product offers a loss-of-function model for the human PAFAH1B3 gene, which encodes the catalytic alpha subunit of platelet-activating factor acetylhydrolase Ib. The polyclonal nature ensures a heterogeneous population of cells with targeted gene disruption, providing a robust system for studying PAFAH1B3-dependent pathways in a lymphoid context.
The Raji cell line is a well-characterized human B lymphocyte model originally isolated from a Burkitt??s lymphoma patient and immortalized by Epstein-Barr virus (EBV). These lymphoblastoid cells grow in suspension, maintain EBV positivity, and are extensively used in immunology and oncology research. Their B-cell lineage makes them particularly relevant for investigating signaling pathways that govern lymphocyte function, survival, and malignant transformation.
PAFAH1B3 functions as a critical enzyme that hydrolyzes platelet-activating factor (PAF), a potent pro-inflammatory phospholipid mediator, into biologically inactive lyso-PAF. This catalytic activity is part of a heterotrimeric complex with PAFAH1B1 (LIS1) and PAFAH1B2. Upstream activators such as inflammatory cytokines (TNF-??, IL-1??) and oxidative stress modulate PAFAH1B3 expression, while its enzymatic action attenuates downstream PAF receptor (PTAFR) signaling. Consequently, PAFAH1B3 limits activation of NF-??B and MAPK/ERK cascades, thereby dampening inflammatory and proliferative responses. Additional regulatory interplay involves the dynein complex and phospholipase C (PLC)-mediated pathways.
In the Raji B-cell lymphoma background, knockout of PAFAH1B3 eliminates enzymatic degradation of PAF, leading to ligand accumulation and sustained PTAFR engagement. This disruption provides a powerful system to examine how unrestrained PAF signaling influences lymphomagenesis, inflammation, and therapeutic vulnerabilities. Given the EBV-positive status of Raji cells, the model also enables exploration of viral oncoprotein interactions with host PAF signaling networks, while also allowing dissection of interconnections between phospholipid metabolism and oncogenic programs.
Researchers can employ these cells to dissect PAF-driven signaling in B-cell malignancies using complementation studies, pharmacological inhibition, and quantitative assays such as Western blotting, RT-qPCR, PAF ELISA, and calcium flux measurements. They are suitable for phenotypic readouts including proliferation, apoptosis, and cytokine profiling, as well as for high-throughput screening of PAF pathway modulators. For additional details or inquiries, please contact Ascent Research.
