The EHBP1L1 Knockout HEK293T Polyclonal Cells comprise a CRISPR/Cas9-edited polyclonal knockout cell population in which the EHBP1L1 gene has been disrupted. This pool of edited cells provides a heterogeneous loss-of-function model for investigating EHBP1L1-mediated endocytic recycling and actin cytoskeleton remodeling without clonal selection, enabling robust studies of gene function in a physiologically relevant cellular context.
The HEK293T host cell line is a widely utilized human embryonic kidney cell derivative that stably expresses the SV40 large T antigen. This immortalized epithelial cell line supports high transfection efficiency and robust heterologous protein expression, making it a standard platform for mechanistic cell biology, signal transduction studies, and viral vector production.
EHBP1L1 encodes an adaptor protein that bridges Rab8 GTPase-positive vesicles to the actin cytoskeleton through direct interaction with Bin1. Functioning downstream of Rab8, CDC42, and the Par complex, EHBP1L1 promotes apical trafficking of membrane proteins and is essential for maintaining epithelial cell polarity. The EHBP1L1 pathway includes Rab8, Bin1, dynamin, actin, and Myo5B, collectively coordinating endocytic recycling and ciliogenesis. Loss of EHBP1L1 disrupts this network, impairing apical membrane protein delivery and actin organization.
In HEK293T cells, which retain epithelial characteristics, EHBP1L1 knockout disrupts polarized trafficking and ciliogenic programs, making this model a valuable tool for dissecting the molecular basis of epithelial morphogenesis and ciliary dysfunction. Although HEK293T cells are not fully polarized in standard culture, they provide a tractable system to study the fundamental aspects of Rab8-EHBP1L1-Bin1 axis-dependent trafficking and its impact on actin dynamics and organelle positioning.
This polyclonal knockout product is suited for a range of applications, including immunofluorescence analysis of actin organization and cilia formation, western blotting for pathway component expression, and co-immunoprecipitation to probe Rab8A/EHBP1L1/Bin1 interactions. It enables mechanistic studies of apical trafficking, drug screening for ciliopathy-related compounds, and investigation of epithelial polarity regulators. For further details, please contact Ascent Research.
