The CCDC120 Knockout Jurkat Polyclonal Cells are a precisely engineered CRISPR/Cas9-edited polyclonal knockout cell population derived from the Jurkat T-lymphoblastoid cell line, designed to ablate the expression of the coiled-coil domain-containing protein CCDC120. This product provides a heterogeneous pool of gene-disrupted cells, reflecting the CRISPR/Cas9-mediated targeted disruption of the CCDC120 locus without clonal selection, thereby offering a robust model for studying loss-of-function effects in a physiologically relevant T-cell context. The polyclonal nature ensures retention of diverse genetic background, minimizing clonal artifacts and enabling population-level analyses of cytoskeletal and adhesion phenotypes.
The Jurkat host cell line is an immortalized human T-lymphocyte model originally established from the peripheral blood of a 14-year-old male with acute T-cell leukemia. These suspension cells are widely employed in biomedical research to investigate T-cell signaling cascades, activation dynamics, and apoptotic mechanisms. Jurkat cells express typical T-cell surface markers and key signaling intermediates, including components of the T-cell receptor complex, making them an ideal platform for dissecting pathways that govern lymphocyte adhesion, migration, and immune synapse formation. Their robust growth characteristics and ease of genetic manipulation further enhance their utility in functional genomics studies.
CCDC120 encodes a putative scaffold protein featuring coiled-coil motifs that facilitate its integration into macromolecular complexes at the actin cytoskeleton?Cplasma membrane interface. It functions as a critical organizer of actin remodeling by interacting with CCDC88A (Girdin), CCDC88C (Daple), and ERM proteins, thereby linking extracellular adhesion signals to Rho GTPase-driven cytoskeletal rearrangements. Downstream, CCDC120 modulates the dynamics of the actin cytoskeleton and integrin adhesion complexes, with its activity converging on pathway components such as RhoA, Rac1, FAK, and Src. Although upstream regulatory mechanisms remain undetermined, CCDC120 likely participates in signal transduction downstream of T-cell activation events, reinforcing its role in the coordination of cell-matrix and cell-cell interactions.
In Jurkat T cells, knockout of CCDC120 disrupts the normal scaffolding of actin networks, leading to profound impairments in cell adhesion and migration??processes essential for T-cell trafficking and immune surveillance. This model is particularly relevant for exploring the molecular basis of T-cell dysfunction in leukemia, as CCDC120??s potential association with leukemogenesis and developmental disorders is under investigation. By eliminating CCDC120 expression, researchers can mechanistically interrogate how this scaffold protein integrates adhesion signaling with cytoskeletal dynamics, potentially revealing vulnerabilities in leukemia cell homing or survival mechanisms.
This CCDC120 knockout polyclonal Jurkat model supports diverse experimental applications, including functional studies of CCDC120 in T-cell biology and the dissection of actin-related pathologies in leukemia. Researchers can employ Western blotting to confirm target protein depletion, immunofluorescence imaging of F-actin to visualize cytoskeletal architecture, quantitative cell adhesion assays to evaluate substrate attachment, and transwell migration chambers to assess chemotactic capacity. Flow cytometric analysis of integrins such as CD11a/CD18 (LFA-1) further enables monitoring of adhesion receptor surface expression. For additional information or to discuss licensing opportunities, please contact Ascent Research.
