The OPHN1 Knockout Raji Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout cell population derived from the Raji human Burkitt lymphoma B lymphocyte line. This loss-of-function model, generated through CRISPR/Cas9-mediated disruption of the OPHN1 gene, enables investigation of oligophrenin-1 function in a lymphoblastoid background without clonal artifacts.
The Raji cell line, established from an 11-year-old male with Burkitt lymphoma, is an EBV-immortalized suspension line expressing B-cell markers. Widely used to study B-cell biology, lymphoma, and immune function, Raji cells offer a genetically tractable host for CRISPR knockouts, facilitating exploration of OPHN1??s roles beyond neurobiology.
OPHN1 encodes a Rho GTPase-activating protein (RhoGAP) that inactivates RhoA, Rac1, and Cdc42, thereby reducing ROCK/LIMK signaling and cofilin phosphorylation to modulate actin dynamics. OPHN1 is recruited to endocytic sites via endophilin-A2 and CIN85, and it can be activated by NMDA receptor, EphB2, and Src kinase pathways. Through Homer1-Shank complexes, it regulates AMPA receptor endocytosis, a process crucial for synaptic plasticity. Disruption of OPHN1 in Raji cells is expected to alter actin cytoskeleton organization and clathrin-mediated trafficking.
In B lymphocytes, OPHN1 knockout permits dissection of Rho GTPase signaling in immune functions such as adhesion, migration, and endocytosis. This model is particularly relevant for Burkitt lymphoma research, as it allows examination of how aberrant actin regulation intersects with oncogenic signaling, including mTOR pathways. The polyclonal knockout thus provides an accessible system to study OPHN1??s non-neuronal functions and potential links to lymphoma pathology.
Research applications include Rho GTPase signaling analysis, endocytosis assays (e.g., transferrin/EGF uptake), cytoskeletal studies via F-actin immunofluorescence, and live-cell imaging. These cells are suitable for Western blotting, RT-qPCR, Rho GTPase activity pull-downs, flow cytometry, and co-immunoprecipitation to map interacting partners such as endophilin and CIN85. For more information, contact Ascent Research.
