The LIN7C Knockout Raji Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout cell population that carries targeted disruption of the LIN7C gene in the human Raji B lymphocyte background. Supplied as a pool of genome-edited cells, this product avoids clonal selection artifacts, enabling robust loss-of-function analyses. The LIN7C locus has been targeted via CRISPR/Cas9-mediated gene disruption, generating a versatile knockout model for functional studies in lymphoid cells.
Raji cells are a well-characterized human Burkitt’s lymphoma B lymphocyte line, immortalized with Epstein-Barr virus and adapted for suspension growth. They express hallmark B cell markers such as CD19, CD20, and surface IgM, and they retain the capacity for antibody production, antigen presentation, and B cell receptor signaling. Raji cells provide a clinically relevant background for exploring B cell biology and lymphomagenesis, and they are amenable to genetic manipulation and high-throughput screening.
LIN7C encodes a PDZ domain-containing scaffold protein that nucleates the apical CRB3/PALS1/PATJ polarity complex at tight junctions. LIN7C directly interacts with PALS1, PATJ, and CRB3, and also associates with ??-catenin, CASK, and VELI proteins. Upstream regulation originates from PKC?? and Frizzled receptors, linking LIN7C to the Par complex (Par3/Par6/aPKC) and the Wnt/PCP pathway. Through these interactions, LIN7C controls the subcellular localization of tight junction proteins like occludin and claudins, orchestrates actin cytoskeleton dynamics, and regulates vesicle trafficking. Disruption of LIN7C consequently dismantles this macromolecular scaffold, compromising cell polarity, barrier integrity, and intracellular transport.
In the Raji B lymphocyte context, LIN7C knockout provides a unique model to investigate non-canonical roles of polarity proteins in hematopoietic cells. While B cells lack canonical tight junctions, the CRB3/PALS1/PATJ complex is implicated in immune synapse formation, integrin-mediated adhesion, and chemokine-directed migration??processes central to B cell activation and lymphoma dissemination. LIN7C disruption may perturb the polarized assembly of signaling molecules at the immune synapse and alter adhesion to endothelial or stromal cells, offering insights into the invasive behavior of malignant B cells.
This knockout model is suitable for a range of applications, including studies of cell polarity in hematological malignancies, B cell adhesion and migration assays, characterization of immune synapse architecture, and drug screening targeting the lymphoma microenvironment. Researchers can validate LIN7C disruption using Western blotting, RT-qPCR, and Sanger sequencing, and perform functional assays such as transwell migration, flow cytometry for adhesion markers (e.g., LFA-1, ICAM-1), co-immunoprecipitation of polarity complex components, and immunofluorescence. The polyclonal format facilitates population-level analyses and avoids clonal bias. For additional technical details or support, please contact Ascent Research.
