The CCDC120 Knockout HAP1 Polyclonal Cells represent a CRISPR/Cas9-edited polyclonal knockout cell population that provides a loss-of-function model for studying the coiled-coil domain-containing protein CCDC120. This gene-edited product is derived from the near-haploid HAP1 cell line through targeted disruption of the CCDC120 gene, resulting in a heterogeneous pool of cells carrying various mutations at the target locus. The polyclonal format ensures a robust genetic background for functional investigations of CCDC120-dependent processes in intracellular trafficking and ciliary biology.
HAP1 is a near-haploid derivative of the KBM-7 chronic myeloid leukemia (CML) cell line, originally isolated from a patient in blast crisis. These cells retain myeloid progenitor characteristics and exhibit a predominantly haploid karyotype, which simplifies gene-editing experiments and minimizes the presence of wild-type alleles. Their leukemic origin and adherent growth properties make them a suitable host for studying trafficking pathways that may contribute to oncogenic signaling and for imaging-based assays and high-throughput screening.
CCDC120 functions as a coiled-coil scaffold protein at the recycling endosome, where it bridges Rab11 GTPases and effector proteins to coordinate cargo sorting and delivery. It directly interacts with RAB11FIP2 and Rab11a to facilitate the recycling of receptors and adhesion molecules from endosomes to the trans-Golgi network and plasma membrane. Additionally, CCDC120 associates with BBS1 and IFT20, linking recycling endosome dynamics to primary cilium assembly via the BBSome. This dual role suggests that CCDC120 may integrate growth factor signaling with ciliary transport, though its upstream regulatory mechanisms remain poorly defined.
Disruption of CCDC120 in HAP1 cells provides a clean background for dissecting endocytic recycling pathways often dysregulated in myeloid malignancies. The leukemic origin of the host line makes this model particularly relevant for examining how abnormal endosomal trafficking supports cancer cell proliferation and survival. Although no monogenic disease is directly associated with CCDC120, its involvement in primary cilium formation and cargo trafficking mechanistically links it to ciliopathy-related processes and tumor progression. Loss of CCDC120 may impair the recycling of growth factor receptors and integrins, thereby altering cell migration and oncogenic signaling.
Researchers can employ this polyclonal knockout population to study endosomal recycling via receptor recycling assays, immunofluorescence staining of Rab11 and EEA1, and co-immunoprecipitation of CCDC120 interaction partners such as RAB11FIP2 and BBS1. Cilium formation assays allow functional analysis of ciliary defects in a myeloid context. Western blotting and RT-qPCR confirm target disruption and downstream pathway changes. The model is suited for high-content screening of trafficking modulators, detailed investigation of primary cilium assembly in cancer cells, and functional mapping of CCDC120 domains. For further information, please contact Ascent Research.
