The KHDRBS2 Knockout HEK293T Polyclonal Cells provide a CRISPR/Cas9-edited polyclonal knockout population in HEK293T cells, enabling loss-of-function studies of the KHDRBS2 gene. This product features targeted gene disruption across a polyclonal background, offering a versatile model for functional genomics and signaling research without clonal isolation.
HEK293T cells are derived from human embryonic kidney tissue and stably express the SV40 large T-antigen, which enables episomal replication of plasmids bearing the SV40 origin of replication. This results in exceptionally high transient transfection efficiency, making them a preferred host for recombinant protein production, lentiviral packaging, and signaling studies. Their robust growth and well-characterized signaling networks provide an ideal backdrop for gene knockout experiments.
KHDRBS2 is a member of the STAR family of RNA-binding proteins that governs alternative splicing and translational control in response to extracellular signals. Upon activation of receptor tyrosine kinases such as EGFR and PDGFR, downstream kinases including Src, Fyn, and Pyk2 phosphorylate KHDRBS2, inducing its relocalization. In the nucleus, it regulates splicing of CD44 and BCL-X, while in the cytoplasm it influences translation of Cyclin D1. It forms complexes with Sam68, hnRNP A1, and SR proteins, and associates with adaptors Grb2 and PLC??1, thereby integrating growth factor pathways with post-transcriptional gene regulation.
Disruption of KHDRBS2 in HEK293T cells creates a model to study its function in tyrosine kinase signaling and RNA processing. The polyclonal knockout captures diverse editing outcomes, enabling assessment of overall gene function without clonal selection bias. This model is relevant for cancer research, given KHDRBS2’s roles in breast, lung, and leukemia, where its splicing activity supports tumorigenesis.
Typical experimental workflows include RT-qPCR to quantify KHDRBS2-dependent splicing isoforms, RNA immunoprecipitation to identify RNA targets, co-immunoprecipitation to map protein interactions, and phospho-signaling analysis to study kinase regulation. Splicing reporter minigene assays provide direct readouts of splicing activity, while cell proliferation and viability assays assess functional consequences. Immunofluorescence can localize KHDRBS2 in response to stimuli. This product is a valuable resource for drug target validation and cancer cell signaling research. For further information or to discuss custom applications, please contact Ascent Research.
