Phospho-EphA2 (Tyr594) Recombinant Rabbit mAb (S-3503-91)

Phospho-EphA2 (Tyr594) is a specific modified form of the receptor tyrosine kinase EphA2 phosphorylated at tyrosine residue 594, a phosphorylation event mediated by ligand (e.g., ephrin-A1) activation or Src family kinases, representing an important indicator of its kinase activity. The activation of EphA2 involves phosphorylation at multiple tyrosine sites, among which Tyr594 is located in the activation loop within the kinase domain, and its phosphorylation is critical for stabilizing the active conformation of the kinase and enhancing its catalytic function. Phosphorylation at this site promotes the binding of EphA2 to downstream signaling molecules such as the p85 subunit of PI3K, thereby activating pro-survival and pro-proliferation pathways including PI3K-AKT and MAPK/ERK, and participating in processes such as angiogenesis, cell migration, and tissue boundary formation during normal development. However, in many malignant tumors (including breast cancer, lung cancer, glioblastoma, etc.), EphA2 is frequently hyperphosphorylated (including at the Tyr594 site), and this aberrant modification is closely associated with enhanced tumor cell invasiveness, epithelial-mesenchymal transition (EMT), and poor prognosis. Therefore, Phospho-EphA2 (Tyr594) not only serves as a functional phosphorylation site reflecting EphA2 kinase activity but is also widely used as a key molecular marker for studying the activation status of the EphA2 signaling pathway and its role in cancer progression, as well as a potential therapeutic intervention target.