The KIF13B Knockout Jurkat Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout cell population derived from the Jurkat human T lymphocyte line. This loss-of-function model features targeted gene disruption of KIF13B, the gene encoding a kinesin motor protein essential for endosomal transport and receptor recycling. The polyclonal format ensures a heterogeneous pool of edited cells, avoiding clonal bias and enabling robust functional studies. Supplied as a ready-to-use stock, these cells streamline experimental workflows in cell biology, immunology, and cancer research.
Jurkat cells are immortalized human T lymphocytes originally isolated from an acute T cell leukemia patient. They retain key T-cell biological properties, including antigen receptor-mediated signaling, cytokine secretion, and integrin-dependent adhesion. As a well-characterized model for adaptive immune responses and T-ALL pathogenesis, Jurkat cells provide a relevant context for investigating KIF13B functions in lymphocyte activation, migration, and malignant transformation.
KIF13B operates as a plus-end-directed microtubule motor that transports Rab11-positive recycling endosomes to the cell surface, delivering integrin ??5??1 and EGFR. Its activity is regulated upstream by integrin ??1 engagement, EGFR stimulation, and the GTPases RAC1, CDC42, Rab5, and Rab11. Downstream, KIF13B-mediated recycling promotes FAK phosphorylation, paxillin recruitment, and actin cytoskeleton remodeling. The motor interacts directly with ??-actin, Rab5, Rab35, and the exocyst complex, integrating endosomal trafficking with microtubule and actin dynamics. Core pathway components include RAB11, RAB5, EHD1, RAC1, CDC42, integrin ??1, FAK, paxillin, and actin, collectively regulating cell adhesion, migration, and signaling.
In T lymphocytes, endosomal recycling is critical for immune synapse assembly, sustained receptor signaling, and polarized migration. KIF13B-dependent transport of integrins and receptors modulates adhesion to antigen-presenting cells and directional motility. Disruption of KIF13B in Jurkat cells likely impairs integrin recycling and surface receptor display, altering T-cell activation thresholds and migration capacity. This model thus offers a powerful tool to study motor protein roles in T-ALL, autoimmune disorders, and leukemia cell metastasis, particularly at the interface of RAC1 signaling and microtubule dynamics.
Applications include quantitative endosomal recycling assays, integrin trafficking analysis during immune synapse formation, and Transwell migration studies to assess invasiveness. The model supports phospho-signaling profiling of FAK and downstream effectors, integrin recycling measurements via flow cytometry or imaging, and T-cell activation assays (e.g., IL-2 ELISA). It is also suitable for screening small-molecule inhibitors of kinesin motors. Researchers can validate KIF13B disruption using Western blotting and RT-qPCR. For additional technical specifications, please contact Ascent Research.
