The KIF13B knockout HEK293T polyclonal cells constitute a CRISPR/Cas9-mediated gene disruption model in which the KIF13B locus is targeted to ablate expression of this kinesin motor protein. This product is a heterogeneous pool of edited cells, not a clonal isolate, designed to enable loss-of-function studies without the confounding effects of single-cell clonal expansion. The polyclonal population provides a robust system for investigating KIF13B-dependent processes, with sufficient cell numbers for high-throughput screening and replicate analyses. By disrupting KIF13B, researchers can dissect the protein’s role in intracellular transport and receptor trafficking across diverse experimental contexts.
HEK293T cells are a widely used human embryonic kidney epithelial line derived from HEK293 cells through stable integration of the SV40 large T antigen. This modification permits episomal replication of transfected plasmids, resulting in elevated protein production and making the line exceptionally suitable for transient transfection, lentiviral packaging, and live-cell imaging. The epithelial origin of HEK293T cells renders them a physiologically relevant host for studying polarized membrane trafficking, cell adhesion, and signal transduction. Their facile genetic manipulation and well-characterized proteome support detailed mechanistic analyses of motor protein function and endosomal sorting pathways.
KIF13B encodes a plus-end-directed microtubule motor that transports Rab11-positive vesicles from the trans-Golgi network to the plasma membrane. The motor binds directly to the active GTP-bound form of Rab11 on vesicle surfaces and moves processively along microtubules through cycles of ATP hydrolysis. KIF13B also interacts with the membrane-associated guanylate kinase scaffold protein DLG1 (SAP97), which couples the motor to cargoes including the mannose-6-phosphate receptor and ??1-integrin. This interaction is modulated by CaMKII- and Src kinase-mediated phosphorylation, linking KIF13B activity to upstream signaling cascades. Additionally, KIF13B associates with PI3P-enriched membranes via the phosphoinositide kinase PIKFYVE, revealing a regulatory nexus that coordinates vesicular cargo selection and delivery to specific plasma membrane domains.
Disruption of KIF13B in HEK293T cells creates a loss-of-function epithelial model that unveils the motor’s contributions to surface receptor localization and cell behavior. In these cells, KIF13B normally governs the plasma membrane delivery of ??1-integrin, thereby influencing focal adhesion dynamics and cell migration??processes frequently hijacked during cancer metastasis. The knockout model therefore enables the study of integrin trafficking, adhesive signaling, and motility in an epithelial context relevant to tumor biology. Moreover, HEK293T cells can be engineered to express immune receptors, permitting reconstitution of immune synapse components to examine how KIF13B-dependent receptor transport affects synapse formation and function, a process implicated in immune disorders.
This polyclonal knockout cell product is suited for a broad spectrum of investigations, including live-cell imaging of vesicle trafficking, quantitative analysis of surface receptor levels by flow cytometry, and co-immunoprecipitation of motor-cargo complexes. Migration and invasion assays with these cells can elucidate the role of KIF13B in metastatic dissemination, while pharmacological screens may identify modulators of KIF13B-dependent transport. The product is also amenable to immunofluorescence-based colocalization studies and RT-qPCR/Western blot validation of downstream targets. For additional technical specifications, pricing, or ordering, please contact Ascent Research.
