Extracellular domain of human ephrin-A4 (amino acids 1-203) was fused to the C-terminal 6X histidine-tagged Fc region of human IgG1.
Biochem/physiol Actions
Member of the ephrin ligand family that binds Eph receptor tyrosine kinases (EphA2, EphA3, EphA4, EphA5, EphA6, EphA7, and Eph8). Involved in pattern formation and morphogenesis.
Member of the ephrin ligand family that binds Eph receptor tyrosine kinases (EphA2, through Eph8); involved in pattern formation and morphogenesis.
Physical form
Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline.
Analysis Note
The biological activity is measured by its ability to compete with biotinylated human Ephrin-A5/Fc chimera for binding with recombinant mouse EphA3/Fc in ELISA.
We previously reported that EphA4, a member of the Eph family of receptor tyrosine kinases, is an important modulator of growth hormone (GH) signaling, leading to augmented synthesis of insulin-like growth factor 1 (IGF1) for postnatal body growth. In the
Questions
Reviews
★★★★★ No rating value
Active Filters
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.