The EPHB6 Knockout Raji Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout cell population derived from Raji B lymphocytes, featuring targeted disruption of the EPHB6 gene. This loss-of-function model provides a heterogeneous pool of cells for robust functional analysis of the kinase-dead ephrin receptor EPHB6 in a human B-cell context. The live polyclonal product is suited for downstream assays investigating ephrin-dependent adhesion, migration, and immune cell biology, with natural cell-to-cell variation that minimizes clonal selection biases.
The Raji host cell line is an Epstein-Barr virus (EBV)-positive lymphoblastoid line derived from a Burkitt lymphoma patient. These cells exhibit characteristic B-lymphocyte features, including surface immunoglobulin and MHC class II molecule expression, and are widely used in B-cell malignancy and immune function studies. Raji cells are a well-established model for investigating lymphomagenesis, viral oncogenesis, and humoral responses. The EBV-positive background adds clinical relevance for exploring tumor cell interactions within the microenvironment and testing therapeutic strategies against B-cell lymphomas.
EPHB6 encodes a kinase-defective receptor that forms heterodimers with kinase-competent Eph receptors such as EPHB1 and EPHB4, critically modulating Eph/ephrin signaling despite lacking catalytic activity. Binding of ephrin-B ligands (EFNB1, EFNB2, EFNB3) activates downstream Src family kinases (Fyn, Yes) and Abl tyrosine kinases (ABL1, ABL2), which regulate Rho GTPases (RhoA, Rac1, Cdc42) and integrin-mediated adhesion. This leads to actin cytoskeleton reorganization and focal adhesion turnover, governing migration and repulsion. Adaptor proteins GRB2 and CRK fine-tune signal amplitude. Knockout of EPHB6 is thus expected to perturb these pathways, offering a tool to dissect kinase-dead receptor function.
In the Raji B-cell context, EPHB6 disruption likely impairs ephrin-dependent adhesion and chemotaxis, altering B-cell trafficking and lymphoid homing. Given its role in actin dynamics and substratum interactions, knockout may affect lymphoma cell invasion and stromal cross-talk. This model is relevant for Burkitt lymphoma and other B-cell malignancies where ephrin signaling drives progression and metastasis. It also enables exploration of kinase-inactive Eph receptors in immune cell compartmentalization in autoimmune disorders.
This polyclonal knockout product is suited for flow cytometric analysis of EPHB6, western blotting for target confirmation, and adhesion assays on ephrin-coated surfaces. Transwell migration/invasion assays quantify motility changes, and co-immunoprecipitation reveals alterations in Eph receptor complexes. Phospho-signaling analyses (e.g., phospho-Abl, phospho-FAK) map pathway perturbations, while RNA-seq uncovers transcriptomic changes. Xenograft models enable in vivo assessment of lymphoma growth and dissemination. For further information, please contact Ascent Research.
