The MOSPD1 Knockout Raji Polyclonal Cells comprise a CRISPR/Cas9-edited polyclonal knockout population with disruption of the MOSPD1 gene in the human Raji B lymphocyte cell line. This mixed population avoids clonal bias and is suitable for applications requiring genetic heterogeneity, including loss-of-function screens, dose-response experiments, and comparative migration studies. By targeting MOSPD1, researchers can dissect its function in leukocyte adhesion, migration, and transendothelial trafficking within a constitutively active B-cell lymphoma background.
The parental Raji line is an EBV-positive B lymphoblastoid cell line derived from Burkitt lymphoma. It constitutively expresses adhesion molecules such as ICAM-1 and LFA-1, making it a robust model for integrin signaling, NF-??B pathway dynamics, and transendothelial migration studies. Raji cells are well-established for investigating B-cell receptor signaling and lymphoma biology, providing a physiologically relevant context for MOSPD1 functional analysis.
MOSPD1 is a transmembrane protein that regulates cell adhesion, cytoskeletal remodeling, and directional migration. It acts downstream of pro-inflammatory cytokines and B-cell receptor signaling via NF-??B activation. MOSPD1 interacts with integrins, tetraspanins, and cytoskeletal proteins to promote LFA-1 activation and actin reorganization, enabling firm adhesion to endothelial ICAM-1, VCAM-1, and PECAM-1. Downstream signaling involves Src family kinases and Rho GTPases, which coordinate lamellipodium formation and chemotaxis. Disruption of MOSPD1 thus uncouples adhesion receptor engagement from cytoskeletal dynamics.
In Raji B lymphoma cells, MOSPD1 knockout impairs transendothelial migration and reduces invasive potential, recapitulating critical aspects of lymphoma dissemination. Because these cells exhibit high baseline adhesion, the knockout model directly reveals MOSPD1-dependent changes in migration dynamics. This is particularly relevant for B-cell lymphoma pathology, where aberrant homing drives disease progression. Additionally, with NF-??B and integrin pathways dysregulated in inflammation and autoimmunity, these cells serve as a platform for therapeutic target exploration.
These polyclonal knockout cells are suited for a variety of experimental applications. Transwell migration assays can quantify the impact of MOSPD1 disruption on chemotaxis across endothelial monolayers, while static adhesion assays measure integrin-dependent binding to immobilized ICAM-1 or VCAM-1. Flow cytometry with activation-specific antibodies detects LFA-1 conformational changes, and immunofluorescence microscopy visualizes F-actin reorganization. Complementary biochemical approaches such as Western blotting and co-immunoprecipitation characterize MOSPD1 protein complexes. Transcriptomic analysis via RNA-seq reveals downstream gene expression changes. The cells also serve in drug screening campaigns for anti-metastatic or anti-inflammatory compounds. For further information or technical support, please contact Ascent Research.
