EFNA1 Human

Ephrin A1 was first identified as a ligand for the Eph receptor family, which are the largest subfamily of receptor tyrosine kinases. These receptors and their ligands are divided into two classes: Ephrin-A (which are glycosylphosphatidylinositol-anchored to the cell membrane) and Ephrin-B (which are transmembrane proteins). Ephrin A1 specifically binds to EphA receptors, initiating bidirectional signaling that affects both the receptor-expressing and ligand-expressing cells .

The recombinant form of Ephrin A1 is produced using human cells, such as HEK293 cells, to ensure proper folding and post-translational modifications. The recombinant human Ephrin A1 comprises 175 amino acids with a predicted molecular mass of approximately 20.8 kDa. Due to glycosylation, it migrates as an approximately 26 kDa band in SDS-PAGE under reducing conditions .

Ephrin A1 is involved in several key biological processes:

1. Angiogenesis: Ephrin A1 plays a critical role in the formation of new blood vessels. It is upregulated in response to hypoxia and interacts with EphA2 receptors on endothelial cells to promote angiogenesis.
2. Neural Development: Ephrin A1 and its receptors are essential for the proper development of the nervous system. They guide the migration of neural crest cells and the formation of neural networks.
3. Cancer Progression: Ephrin A1 is implicated in the progression of various cancers. It can influence tumor growth, invasion, and metastasis by modulating cell adhesion and migration.

Recombinant human Ephrin A1 is typically produced in a lyophilized form and can be reconstituted in a suitable buffer for experimental use. It is often used in research to study cell signaling pathways, particularly those involved in cancer and developmental biology. The protein’s activity is measured by its binding ability in functional assays, such as ELISA, where it binds to EphA receptors .

Recombinant human Ephrin A1 is stable for up to twelve months when stored at -20°C to -80°C under sterile conditions. It is recommended to aliquot the protein to avoid repeated freeze-thaw cycles, which can degrade its activity .