Recombinant Human EphA8 Fc Chimera Protein, CF

Recombinant Human EphA8 Fc Chimera Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: EphA8

EphA8, also known as Hek3 and Eek, is a 120 kDa glycosylated member of the Eph family of transmembrane receptor tyrosine kinases (1, 2). The A and B classes of Eph proteins are distinguished by Ephrin ligand binding preference but have a common structural organization. EphA4 binds and is activated by class A Ephrins but not class B Ephrins (3, 4). Eph-Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression. The 512 amino acid (aa) extracellular domain (ECD) of human EphA8 contains an N-terminal Ephrin binding region, a cysteine-rich region, and two fibronectin type III domains (FnIII). The 442 aa cytoplasmic domain contains the tyrosine kinase domain and a sterile alpha motif (SAM) (5). Within the ECD, human EphA8 shares 97% aa sequence identity with mouse and rat EphA8. EphA8 is expressed in neurons in the mesencephalon of the developing brain, particularly in the rostral tectum and the superior colliculus (6-8). It is enriched at the tips of neurite processes and plays a role in projection of superior colliculus axons through the posterior commissure (7, 9). Its expression enhances neurite extension by means of a mechanism that does not require catalytic activity of the tyrosine kinase domain (10). Ephrin-mediated activation of the EphA8 kinase induces phosphorylation of tyrosine residues in the cytoplasmic domain, leading to association with signaling and scaffolding proteins and inhibition of cell-cell adhesion (4, 9, 11). Ligand binding can also promote the Integrin-mediated cellular adhesion to Fibronectin (12). This function, like the enhancement of neurite extension, does not require activation of the kinase domain (12).

Related Research Areas

• Ephrin Ligands and Eph Receptors
• Receptor Tyrosine Kinases (RTKs)