The DPYSL2 Knockout Jurkat Polyclonal Cells represent a CRISPR/Cas9-edited polyclonal knockout population of Jurkat cells, engineered to disrupt the DPYSL2 gene. DPYSL2 encodes collapsin response mediator protein 2 (CRMP2), a key regulator of cytoskeletal dynamics. This product provides a heterogeneous pool of knockout cells, enabling loss-of-function studies without clonal selection artifacts. The polyclonal format reflects the diversity of knockout alleles generated by non-homologous end joining following Cas9-mediated double-strand breaks, offering a robust model for investigating CRMP2 function in a T-cell context. These cells are suitable for a broad range of assays, including migration, signaling, and protein interaction studies.
The Jurkat host cell line is an immortalized human T lymphocyte line derived from an acute T cell leukemia patient. Jurkat cells are extensively utilized in immunological research to dissect T cell receptor (TCR) signaling, activation, apoptosis, and cytokine production. Their easy propagation and well-characterized signaling pathways make them an ideal chassis for gene-editing studies. The disruption of DPYSL2 in this background provides a means to directly interrogate the cytoskeletal control mechanisms that govern T cell functional responses.
DPYSL2/CRMP2 is a multifunctional phosphoprotein that regulates microtubule polymerization and actin reorganization. It functions downstream of the SEMA3A receptor complex (NRP1/PLXNA) and the TCR/CD3 complex. Upon activation, kinases including LCK and ZAP70 phosphorylate CRMP2, modulating its interactions with tubulin, actin, and regulatory partners such as CRMP1, CRMP3, CRMP4, DPYSL5, LIS1, and kinesin-1. CRMP2 also influences small GTPases RhoA, Rac1, and Cdc42, and the transcription factor NFAT, thereby linking guidance and activation cues to cytoskeletal remodeling and gene expression. Key signaling axes include SEMA3A-NRP1/PLXNA-CRMP2-microtubule and TCR-LCK-ZAP70-CRMP2-actin.
In Jurkat cells, CRMP2 is critical for T cell polarization, migration, and immunological synapse formation. Loss of DPYSL2 disrupts cytoskeletal reorganization at the immune synapse, impairing TCR signaling. This knockout model enables dissection of CRMP2-dependent pathways in processes such as chemokine-induced migration and integrin-mediated adhesion.
These DPYSL2 knockout polyclonal cells are well-suited for applications including Transwell migration assays to study T cell motility, microtubule polymerization assays to assess cytoskeletal dynamics, and flow cytometric analysis of activation markers like CD69 and IL-2. Co-immunoprecipitation can be used to examine CRMP2 protein interactions, and knockout rescue experiments allow functional validation. The model also supports drug screening efforts targeting neuroimmune disorders or cancer metastasis. For further technical information or to inquire about custom cell engineering services, please contact Ascent Research.
