protein

Ephrin-A5/EFNA5 Protein, Rat (HEK293, His)

HY-P73014

2 μg;10 μg;50 μg;100 μg;500 μg

35;60;165;280;785 USD

Ephrin-A5/EFNA5 Protein, Rat (HEK293, His)

proteins

HEK293

2 μg;10 μg;50 μg;100 μg;500 μg

35;60;165;280;785 USD

The Ephrin-A5/EFNA5 protein is an important cell surface ligand that plays an important role in neuronal, vascular, and epithelial development. It binds to Eph receptors, initiating bidirectional signaling and regulating intercellular adhesion, cytoskeletal organization, and lens transparency. Ephrin-A5/EFNA5 Protein, Rat (HEK293, His) is the recombinant rat-derived Ephrin-A5/EFNA5 protein, expressed by HEK293 , with C-His labeled tag. The total length of Ephrin-A5/EFNA5 Protein, Rat (HEK293, His) is 182 a.a., with molecular weight of ~27 kDa.

Rat

The Ephrin-A5/EFNA5 protein, a cell surface GPI-bound ligand for Eph receptors, plays a crucial role in neuronal, vascular, and epithelial development, where Eph receptors are essential for migration, repulsion, and adhesion. EFNA5 binds promiscuously to Eph receptors on adjacent cells, initiating contact-dependent bidirectional signaling, with forward signaling downstream of the receptor and reverse signaling downstream of the ephrin ligand. When bound to its cognate receptor, EFNA5 induces compartmentalized signaling within a caveolae-like membrane microdomain, requiring the activity of the Fyn tyrosine kinase. It activates the EPHA3 receptor to regulate cell-cell adhesion and cytoskeletal organization, and in association with EPHA2, may play a role in shaping lens fiber cells and maintaining lens transparency. Additionally, EFNA5 stimulates axon fasciculation and mediates communication between pancreatic islet cells, regulating glucose-stimulated insulin secretion through its interaction with EPHA5. It is also a cognate ligand for EPHA7, influencing brain development by modulating cell-cell adhesion and repulsion. Furthermore, EFNA5 interacts with EPHA8, activating this receptor, and forms a ternary complex with EPHA3 and ADAM10, mediating extracellular domain shedding and regulating the internalization and function of the EFNA5-EPHA3 complex.

Ephrin-A5; AL-1; EPH-related receptor tyrosine kinase ligand 7; LERK-7; EFNA5; EPLG7

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.5.

Room temperature in continental US; may vary elsewhere.