Recombinant Human Ephrin A3 protein (denatured) (His tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Ephrin A3 also known as Ephrin-A3 or EFNA3 is a member of the ephrin family that interacts with Eph receptors which are a group of tyrosine kinase receptors. Ephrin A3 has a mass of approximately 24 kDa. It is expressed in various tissues including the brain where it plays a significant role in neural development. The expression pattern of Ephrin A3 suggests its involvement in a wide range of physiological processes.

Biological function summary

Ephrin A3 acts as an important regulator in cell communication and spatial organization within the brain's neuronal network. It forms a complex with Eph receptors on adjacent cells leading to bidirectional signaling necessary for processes like axon guidance and synaptic plasticity. Ephrin A3's ability to guide axons is important for neural pathfinding during development. It also participates in the clustering of neurons required for the formation of precise neural circuits.

Pathways

Ephrin A3 is a significant player in the Eph/ephrin signaling pathway which influences the dynamics of cell adhesion shape and movement. It is closely related to EphA3 and EphA4 receptors through these pathways. The signaling influences the cytoskeleton affecting cell migration and tissue boundary formation. Additionally Ephrin A3 interacts within the Rho family of GTPase signaling pathways that regulate cytoskeletal rearrangements impacting cellular morphology and motility.

Ephrin A3 is implicated in conditions like cancer and neurological disorders. Aberrant expression or signaling of Ephrin A3 contributes to tumor progression and metastasis potentially through its role in modifying cell adhesion and migration. Through its involvement in the neural network it may also relate to neurodegenerative diseases. The interaction with proteins like EphA2 in cancer highlights its potential as a therapeutic target. Understanding these interactions opens pathways for strategies to modulate its function in disease contexts.