The ANXA2 Knockout HEK293T Polyclonal Cells are a CRISPR/Cas9-edited population of HEK293T cells in which the ANXA2 gene has been disrupted, generating a loss-of-function model devoid of functional ANXA2 protein. This polyclonal knockout product maintains genetic heterogeneity, providing a robust system for bulk biochemical and functional studies without the confounds of clonal selection. The cell population is ideal for investigating ANXA2-dependent processes in a highly transfectable background.
HEK293T cells are a human embryonic kidney epithelial line that stably expresses the SV40 large T antigen, enabling episomal replication of plasmids containing the SV40 origin of replication. This feature facilitates high-level recombinant protein expression and efficient viral production, establishing HEK293T as a preferred host for transient transfection, lentiviral packaging, and signaling analyses. Their epithelial origin and well-characterized growth properties make them highly amenable to genome editing applications.
ANXA2 encodes a calcium-dependent phospholipid-binding protein that forms a heterotetrameric complex with S100A10, localizing to the plasma membrane to serve as a receptor for tissue plasminogen activator (tPA) and plasminogen. This interaction promotes plasmin generation, driving fibrinolysis and extracellular matrix degradation. ANXA2 activity is regulated upstream by HIF1A, Src kinase, protein kinase C (PKC), calcium flux, epidermal growth factor (EGF), transforming growth factor-beta (TGF-??), and glucocorticoids, and it influences downstream actin cytoskeleton remodeling and cell surface proteolysis. Key molecular partners include actin, phosphatidylserine, and fibrinolysis components such as tPA and plasminogen. Disruption of ANXA2 impairs plasminogen activation, compromising cell migration and invasion capacity.
In the HEK293T context, ANXA2 knockout abolishes cell surface ANXA2/S100A10 complex assembly, attenuating plasmin-mediated proteolysis and providing a tractable model for epithelial membrane dynamics, exocytosis, and angiogenesis research. This system recapitulates functional ANXA2 deficiency, making it relevant for studying pathological conditions linked to dysregulated fibrinolysis and cell motility, including cancer metastasis, acute promyelocytic leukemia, thrombosis, and antiphospholipid syndrome. The high transfectability of HEK293T cells further supports rescue experiments and protein interaction mapping.
These polyclonal knockout cells are suited for fibrinolysis assays such as cell surface plasmin generation measurements, as well as cancer cell migration and invasion studies using Boyden chamber or wound healing assays. Western blotting and immunofluorescence microscopy enable detection and localization of ANXA2 and downstream targets, while co-immunoprecipitation validates interactions with S100A10 or tPA. Flow cytometry facilitates quantitative assessment of surface ANXA2 loss. Additional applications include drug target validation, signal transduction dissection, and angiogenesis research. For further information, please contact Ascent Research.
