LAMA3 Knockout Raji Polyclonal Cells are a CRISPR/Cas9-edited pool of Raji B lymphocytes with targeted disruption of the LAMA3 gene. This polyclonal knockout model offers a consistent loss-of-function background in a well-characterized Burkitt lymphoma host, facilitating reliable studies of LAMA3-dependent mechanisms without the limitations of clonal selection.
The Raji cell line, an EBV-immortalized Burkitt lymphoma suspension culture, is a fundamental model for B cell biology and humoral immunity. It exhibits constitutive NF-??B activity and latent viral gene expression, recapitulating key features of aggressive B cell malignancies. Raji cells?? genetic malleability and streamlined culture protocols make them a preferred host for CRISPR/Cas9-mediated gene editing, enabling functional interrogation of genes in a lymphoma-relevant context.
LAMA3 encodes the alpha-3 chain of laminin-332, which heterotrimerizes with LAMB3 and LAMC2 to form a cruciform matrix protein that binds collagen VII and integrin receptors ??3??1 and ??6??4. Integrin ligation triggers FAK autophosphorylation, recruiting Src and adapter proteins, which activate downstream PI3K-Akt and Ras-Raf-MEK-Erk modules. This signaling axis is also regulated by upstream inputs from TP63, TGF-??, and EGF pathways. Knockout of LAMA3 disrupts laminin-332 assembly, leading to loss of integrin-mediated FAK activation, attenuated Akt phosphorylation, and reduced Erk signaling, culminating in impaired cell adhesion, migration, and survival.
In Raji cells, although laminin-332 is not a canonical B cell product, ectopic or activation-induced LAMA3 expression may influence lymphoma cell adhesion to stromal elements or migration within lymphoid tissues. This knockout population thus facilitates exploration of non-conventional laminin-332 roles in B cell malignancies, including potential contributions to drug resistance and tumor dissemination. It also serves as a comparative platform for junctional epidermolysis bullosa mechanistic studies, where LAMA3 loss causes dermal-epidermal separation.
Typical assays include Western blotting and RT-qPCR for knockout validation, immunofluorescence and flow cytometry for integrin profiling, cell adhesion and transwell migration assays to assess functional deficits, and phospho-FAK/phospho-Akt analysis to map signaling changes. High-throughput drug screening targeting integrin-laminin interactions and RNA-seq-based transcriptomics are also readily performed. For further details and ordering, please contact Ascent Research.
