EPH receptor A4 (ephrin type-A receptor 4); also known as EphA4; belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family which 16 known receptors (14 found in mammals) are involved: EPHA1; EPHA2; EPHA3; EPHA4; EPHA5; EPHA6; EPHA7; EPHA8; EPHA9; EPHA10; EPHB1; EPHB2; EPHB3; EPHB4; EPHB5; EPHB6. The Eph family of receptor tyrosine kinases (comprising EphA and EphB receptors) has been implicated in synapse formation and the regulation of synaptic function and plasticity6. EphA4 is enriched on dendritic spines of pyramidal neurons in the adult mouse hippocampus; and ephrin-A3 is localized on astrocytic processes that envelop spines. Eph receptor−mediated signaling; which is triggered by ephrins7; probably modifies the properties of synapses during synaptic activation and remodeling. Ephrin receptors are components of cell signalling pathways involved in animal growth and development; forming the largest sub-family of receptor tyrosine kinases (RTKs). The extracellular domain of an EphA4 interacts with ephrin ligands; which may be tethered to neighbouring cells. Ligand-mediated activation of Ephs induce various important downstream effects and Eph receptors have been studied for their potential roles in the development of cancer.
1. The specific activity was determined to be 17 nmol/min/mg using Poly(Glu:Tyr) 4:1 as substrate.2. Measured by its binding ability in a functional ELISA. Immobilized human EPHA4 (aa 570-986)at 10 µg/ml (100 ?l/well) can bind biotinylated human EphrinA5-His with a linear range of 0.625-5.0 µg/ml.
Endotoxin:
<1.0 EU per µg of the protein as determined by the LAL method.
Protein Construction:
A DNA sequence encoding the human EPHA4 (P54764) (Ser570-Val986) was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.
