The KIF13B Knockout HeLa Polyclonal Cells represent a CRISPR/Cas9-edited polyclonal knockout cell population in which the KIF13B gene has been disrupted to create a loss-of-function model. These polyclonal knockout cells are derived from the widely used HeLa cervical adenocarcinoma cell line and provide a heterogeneous pool of edited alleles, facilitating the study of KIF13B-dependent processes without clonal selection artifacts. This product is supplied as a ready-to-use polyclonal pool, enabling immediate application in functional assays.
The host HeLa cell line is an HPV18-immortalized human cervical epithelial cell line that has been a foundational model in cancer biology and cell biology for decades. Its robust growth, ease of transfection, and well-characterized signaling networks make it an ideal system for studying cytoskeletal dynamics, cell migration, and endosomal trafficking. The epithelial origin and transformed nature of HeLa cells render them particularly suitable for investigations into cancer cell motility and invasion.
KIF13B encodes a plus-end-directed microtubule motor protein belonging to the kinesin-3 family, which functions as a key mediator of endosomal vesicle transport and integrin recycling. The motor protein is activated downstream of PI3K-AKT signaling through interaction with phosphatidylinositol (3,4,5)-trisphosphate (PIP3), and it associates with Rab11-positive recycling endosomes via adaptor proteins such as AP-1 and FIP3, as well as Syntaxin 13. KIF13B-powered transport delivers integrin alpha5/beta1 heterodimers from perinuclear recycling endosomes to the plasma membrane, thereby promoting the formation of cell protrusions and facilitating cell migration. In the absence of functional KIF13B, endosomal trafficking is impaired, integrin surface levels are reduced, and cell motility is compromised.
In the HeLa cell context, KIF13B loss disrupts the normal recycling of integrins and the spatial organization of endosomal compartments, directly impacting the migratory and invasive capacity of these epithelial cancer cells. Given the reliance of metastatic dissemination on dynamic integrin trafficking and actin-driven protrusion, this knockout model offers a tractable system to dissect the molecular underpinnings of tumor cell invasion. Moreover, the well-defined PI3K-AKT pathway in HeLa cells provides an opportunity to examine how oncogenic signaling converges on KIF13B-dependent membrane trafficking to drive pathological cell migration.
Researchers can employ these polyclonal knockout cells in a variety of assays, including wound healing and transwell migration/invasion assays to quantify motility defects, integrin recycling assays using antibody-based internalization and recycling protocols, immunofluorescence staining for Rab11-positive endosomes, and live-cell imaging of vesicle transport. The cells are also suitable for western blotting to assess downstream effectors of the PI3K-AKT axis and for phospho-AKT signaling analysis. Potential applications extend to drug sensitivity screens for motility inhibitors, cytoskeletal dynamics studies, and cancer metastasis research. For further technical information, please contact Ascent Research.
