The DUSP3 Knockout Raji Polyclonal Cells constitute a CRISPR/Cas9-edited polyclonal knockout cell population originating from the Raji human Burkitt lymphoma B lymphocyte line. This pooled population carries heterogeneous disruptions of the DUSP3 locus, leading to loss of functional dual-specificity phosphatase 3 protein. The polyclonal format provides a genetically diverse loss-of-function model suitable for population-level studies of signaling dynamics, eliminating the need for single-cell cloning and minimizing clonal artifacts.
Raji cells are an Epstein-Barr virus (EBV)-positive B lymphocyte line derived from a Burkitt lymphoma patient. They grow in suspension, express characteristic B cell surface markers, and are extensively employed in research on B cell biology, lymphomagenesis, and immunology. Their robust proliferation and well-characterized signal transduction networks make Raji cells an ideal host for studying the roles of regulatory phosphatases in malignant B cells.
DUSP3 is a dual-specificity phosphatase that dephosphorylates tyrosine and serine/threonine residues on mitogen-activated protein kinases (MAPKs) ERK1/2, JNK1/2/3, and p38??, as well as signal transducer and activator of transcription 5 (STAT5A/STAT5B), thereby functioning as a negative regulator of MAPK and JAK-STAT cascades. In this knockout model, CRISPR-mediated disruption of DUSP3 abolishes its catalytic activity, resulting in hyper-phosphorylation and sustained activation of these kinases. DUSP3 also interacts with and dephosphorylates the epidermal growth factor receptor (EGFR), insulin receptor substrate-1 (IRS1), and the adaptor protein paxillin. The loss of DUSP3 therefore amplifies signaling downstream of B cell receptor (BCR) engagement, cytokine receptors, and growth factor receptors, accelerating pathways that converge on transcription factors such as ELK1, c-FOS, c-JUN, and regulators of proliferation and apoptosis including cyclin D1, Bcl-xL, and MYC.
In the context of Raji B cells, DUSP3 knockout enhances the cell??s sensitivity and response to BCR crosslinking and cytokine stimulation, mirroring hyperactive signaling states found in aggressive lymphomas. The sustained activation of MAPK modules promotes transcriptional programs that drive proliferation and survival, potentially contributing to lymphomagenesis. Because DUSP3 can act as either a tumor suppressor or an oncogene depending on cellular context, this model enables dissection of its dual roles in B cell malignancies. The elevated phospho-signaling state also provides a tractable platform for screening kinase inhibitors targeting components of the RAS-RAF-MEK-ERK and JAK-STAT axes.
Researchers can employ DUSP3 knockout Raji polyclonal cells for a broad spectrum of experimental applications, including B cell signaling studies, lymphoma and leukemia research, immune checkpoint regulation, and drug target validation. Typical assays include Western blot detection of phosphorylated ERK, JNK, p38, and STAT5; RT-qPCR quantification of DUSP3 and downstream targets; flow cytometric assessment of proliferation (Ki-67) and apoptosis (Annexin V); phospho-signaling antibody arrays; and co-immunoprecipitation of DUSP3 with ERK2. The knockout cells are also suited for B cell activation assays and cytokine ELISA analyses. For further information, please contact Ascent Research.
