The DOCK2 Knockout HCT 116 Polyclonal Cells represent a CRISPR/Cas9-edited polyclonal knockout cell population derived from the human colorectal carcinoma cell line HCT 116, engineered to disrupt the DOCK2 gene and establish a loss-of-function model. This polyclonal pool comprises a heterogeneous mix of edited alleles, enabling robust and reproducible assessment of DOCK2 deficiency without clonal isolation. The disruption of target gene expression is achieved via CRISPR/Cas9-mediated gene editing, providing a powerful tool for investigating DOCK2-dependent signaling pathways in a cancer-relevant epithelial context. As a research-grade reagent, this knockout population is suitable for a broad range of functional assays, including migration, invasion, and cytoskeletal dynamics studies, where endogenous DOCK2 activity is critical.
HCT 116 is a widely utilized human colorectal adenocarcinoma epithelial cell line characterized by microsatellite instability (MSI), a KRAS G13D activating mutation, and wild-type TP53 status. This genetic background renders the cells particularly valuable for studying oncogenic signaling, tumor cell motility, and responses to targeted therapies. The epithelial morphology and adherent growth properties of HCT 116 facilitate high-resolution imaging of actin cytoskeleton rearrangements and cell migration. In the context of DOCK2 knockout, this host line permits dissection of Rac1-dependent migratory mechanisms that may operate in parallel or downstream of mutant KRAS-driven pathways, offering insights into colorectal cancer invasion and metastasis.
DOCK2 encodes a guanine nucleotide exchange factor (GEF) that specifically activates Rac1 by catalyzing the exchange of GDP for GTP. Upon activation, Rac1 orchestrates actin polymerization and cytoskeleton remodeling via downstream effectors including PAK1, the WAVE complex, and the Arp2/3 complex. DOCK2 functions in a multiprotein complex with ELMO1 and is regulated by upstream signals from chemokine receptors (e.g., CXCR4, CCR7), T cell receptors, G protein-coupled receptors, and growth factor receptors. The canonical pathway proceeds as DOCK2 ?? ELMO1 ?? Rac1 ?? PAK1 ?? actin polymerization. Additionally, DOCK2 interacts with CRK and VAV, further integrating signals that control cell polarity, lamellipodia formation, and directed migration. Knockout of DOCK2 thus abrogates Rac1-dependent signaling, impairing both immune cell function and, in epithelial tumors, invasive capacity.
In HCT 116 cells, DOCK2 knockout provides a unique experimental system to disentangle the contributions of Rac1-mediated actin dynamics from other oncogenic pathways, such as those driven by mutant KRAS. Given the established role of Rac1 in colorectal cancer progression, loss of DOCK2 is expected to attenuate cell migration and invasion, making this polyclonal knockout population an ideal model for mechanistic studies. The MSI status and intact TP53 further allow exploration of DNA damage responses and genomic instability in the context of impaired cytoskeletal regulation. Moreover, because DOCK2 is a key mediator in immune cells, this model can be employed to study tumor?Cimmune cell interactions in co-culture or in vivo settings, providing a platform for translational immuno-oncology research.
This DOCK2 knockout product is designed for a variety of advanced applications, including quantitative cell migration and invasion assays, Rac1 GTPase activation assays to assess effector engagement, Western blotting for DOCK2 and downstream targets like PAK1, immunofluorescence analysis of actin cytoskeleton reorganization, and co-immunoprecipitation to examine DOCK2 complex formation with ELMO1 or RAC1. Researchers investigating chemokine signaling, cytoskeletal dynamics, or calcium flux in cancer cells will find this model particularly valuable. Additionally, it can be used in drug response screens evaluating inhibitors of cell motility or Rac1 activation, and in tumor microenvironment modeling when combined with immune cell components. For further details on genetic background, quality control, and technical support, please contact Ascent Research.
