The DTNB Knockout Jurkat Polyclonal Cells comprise a CRISPR/Cas9-edited polyclonal population of Jurkat T lymphocytes bearing targeted disruption of the DTNB locus, which encodes beta-dystrobrevin. This knockout model is generated using CRISPR/Cas9-mediated gene disruption in Jurkat cells, yielding a heterogeneous pool of modified cells suitable for functional studies of dystrobrevin deficiency. The polyclonal nature preserves genetic diversity across the edited population, enabling robust assessment of DTNB-dependent phenotypes without clonal selection artifacts. The product is supplied as a ready-to-use suspension culture, validated for loss of target protein expression, and optimized for downstream applications in signal transduction, adhesion, and neuromuscular disease research.
The parental Jurkat cell line is an immortalized human T-lymphocyte model derived from the peripheral blood of a male patient with acute T-cell leukemia (clone E6-1). Jurkat cells are extensively utilized to investigate T-cell receptor (TCR) signaling, immune synapse assembly, and lymphocyte adhesion and migration. As suspension cells, they provide a tractable system for high-throughput screening, molecular biochemistry, and imaging-based assays. Their T-cell origin makes them particularly relevant for examining dystrophin-associated glycoprotein complex (DGC) functions in immune cell biology, where the DGC??s role remains incompletely defined.
DTNB encodes beta-dystrobrevin, a scaffolding component of the DGC that physically links the actin cytoskeleton to the extracellular matrix via interactions with dystrophin, utrophin, alpha- and beta-dystroglycan, the sarcoglycan complex, and syntrophins. Beta-dystrobrevin binds directly to dystrophin and syntrophin isoforms, recruiting signaling molecules such as neuronal nitric oxide synthase (nNOS) and the adaptor Grb2. Consequently, DTNB integrates signals from integrin engagement, laminin binding, and TCR activation, and couples them to downstream effectors including PI3K/AKT, MAPK/ERK, FAK, and Rho GTPases. Through these interactions, beta-dystrobrevin modulates actin remodeling and membrane stability, thereby influencing cell adhesion, migration, and signal transduction.
Disruption of DTNB in Jurkat T cells is expected to impair the assembly or stability of the DGC, leading to defective linkage between the actin cytoskeleton and the extracellular matrix. This deficiency may alter TCR-induced signaling cascades, integrin-mediated adhesion, and cellular motility, providing a context-dependent model to dissect DGC function in lymphocytes. The Jurkat background enables investigation of dystrobrevin??s role in immune synapse formation and T-cell activation, which are critical for adaptive immunity. As a non-muscle cell system, this knockout model uniquely facilitates studies of dystrobrevin outside its traditional muscular context, offering insights into the broader roles of the DGC in cell biology and disease.
This polyclonal knockout product is ideally suited for functional studies of DGC composition and dynamics in immune cells, including Western blot confirmation of complex disruption, immunofluorescence localization of DGC components, and quantitative adhesion and migration assays. It supports phospho-signaling analysis of AKT and ERK activation following TCR stimulation, co-immunoprecipitation of residual complex interactions, and flow cytometric assessment of integrin surface expression. Additionally, the model enables transcriptomic profiling via RNA-seq to uncover global gene expression changes resulting from DTNB loss, and serves as a platform for drug screening targeting dystrobrevin-dependent pathways in muscular dystrophy. For technical inquiries and ordering information, please contact Ascent Research.
