The KIF13B Knockout NCI-H1975 Polyclonal Cells consist of a CRISPR/Cas9-edited polyclonal population derived from the NCI-H1975 human lung adenocarcinoma cell line, designed to disrupt the expression of the KIF13B gene. This polyclonal knockout model provides a heterogeneous loss-of-function system for studying the role of KIF13B in intracellular transport and cancer cell behavior. The knockout cells are generated using CRISPR/Cas9-mediated gene disruption, resulting in a mixed pool of edited alleles without clonal selection, thereby preserving biological variability relevant to population-level studies.
The parental NCI-H1975 cell line is a well-characterized model of non-small cell lung carcinoma (NSCLC) derived from a metastatic site of a female patient with adenocarcinoma histology. These cells harbor activating mutations in EGFR (L858R/T790M) and a PIK3CA G118D mutation, conferring resistance to first-generation EGFR tyrosine kinase inhibitors and dysregulated PI3K/AKT signaling. NCI-H1975 cells are extensively employed to investigate mechanisms of acquired drug resistance, tumor cell invasion, and metastasis in lung adenocarcinoma.
KIF13B encodes a plus-end-directed kinesin-3 motor that transports vesicles and organelles along microtubules. At recycling endosomes, KIF13B is recruited by activated RAB11 and RAB11FIP2, driving the surface delivery of integrin-containing vesicles as well as transferrin and LDL receptors. Its activity is modulated by upstream factors, including Aurora A kinase, PI3K/AKT signaling, and integrin engagement. KIF13B additionally interacts with ARF6, the PI3K p85 subunit, F-actin, and myosin V, thereby linking microtubule-based transport to actin remodeling during cell adhesion, migration, and cytokinesis.
In the context of NCI-H1975 cells, KIF13B is implicated in metastatic processes due to its role in integrin trafficking, which governs cell-matrix adhesion and directed migration. Disruption of KIF13B in this metastatic lung adenocarcinoma background allows researchers to dissect the contribution of kinesin-dependent trafficking to EGFR inhibitor-resistant cancer cell invasion. This model is particularly valuable for exploring how altered vesicular transport intersects with oncogenic signaling pathways to promote tumor dissemination, and for identifying vulnerabilities that may be exploited therapeutically.
These polyclonal knockout cells are suitable for a range of functional assays, including Western blotting and RT-qPCR to confirm KIF13B depletion, wound healing and transwell migration assays to assess motility, and immunofluorescence microscopy to examine integrin localization and microtubule organization. Co-immunoprecipitation studies can verify disruption of the KIF13B?CRAB11 interaction, while phospho-AKT analysis offers insight into pathway crosstalk. Researchers may also employ this model in high-throughput screens for anti-metastatic compounds or in functional genomic studies of kinesin motor proteins. For additional product information or technical support, please contact Ascent Research.
