EPHA2 Knockout Cell Line (HEK 293)

The choice depends on whether you are studying EPHA2's role as a class A Eph family RTK or modeling its functions in cancer biology and emerging EPHA2-targeted therapeutic strategies. The Knockout line is the standard tool for asking whether EPHA2 is required for these processes — EPHA2 is the most-characterized EphA subfamily receptor with established roles in tumor angiogenesis, cancer cell migration, and emerging functions as a cancer therapy target; EPHA2 binds ephrin-A1 with high affinity, and EPHA2 overexpression correlates with poor prognosis in multiple cancers. Overexpression is useful for studying EPHA2 gain-of-function effects. For cancer biology research, the EDITGENE EPHA2 Knockout in HEK293 is a workhorse mechanistic platform — HEK293 supports systematic structure-function studies. Rescue with wild-type or kinase-dead EPHA2 is the standard specificity control. The knockout is a critical specificity tool for anti-EPHA2 antibodies, EPHA2-targeted ADCs, and emerging Eph-targeted cancer therapeutics — EPHA2 has been explored as a target for ADC development in multiple cancer types.

Primary applications: • Ephrin-A1 binding and signaling: ephrin-A1-Fc stimulation followed by phospho-EPHA2 (Y594, Y772) Western blot analysis. • Cancer biology: cell migration, invasion, and angiogenesis assays given EPHA2's emerging cancer roles. • EPHA2-targeted ADC specificity: critical genetic control for anti-EPHA2 antibody-drug conjugates in cancer drug development. • EphA family dissection: parallel analysis with EPHA6 Knockout in HAP1 (also available) for cross-subfamily characterization. EDITGENE recommends this HEK293-based model for biochemical EPHA2 research and structure-function studies.

Yes. EPHA2 rescue experiments are well-established for cancer research: • Construct design: use a codon-modified EPHA2 sequence with a small intracellular C-terminal tag (FLAG, HA). EPHA2 has the canonical Eph architecture — preserve all elements. • Surface localization validation: confirm plasma membrane localization before ephrin-A binding studies. • Kinase-dead rescue: K646A mutation in the ATP-binding lysine abolishes catalytic activity. • Functional readout: rescue should restore ephrin-A1-induced phospho-EPHA2 (Y594, Y772) and downstream signaling. HEK293 transduces efficiently with lentivirus and supports stable rescue line generation.