Mouse EphA4/Eph Receptor A4 (Fc Tag) recombinant protein

Mouse EphA4/Eph Receptor A4 (Fc Tag) recombinant protein

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Receptor tyrosine kinase which binds membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI-anchored ephrin-A and transmembrane ephrin-B ligands including EFNA1 and EFNB3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity. Plays an important role in the development of the nervous system controlling different steps of axonal guidance including the establishment of the corticospinal projections. May also control the segregation of motor and sensory axons during neuromuscular circuit development. In addition to its role in axonal guidance plays a role in synaptic plasticity. Activated by EFNA1 phosphorylates CDK5 at 'Tyr-15' which in turn phosphorylates NGEF regulating RHOA and dendritic spine morphogenesis. In the nervous system, plays also a role in repair after injury preventing axonal regeneration and in angiogenesis playing a role in central nervous system vascular formation. Additionally, its promiscuity makes it available to participate in a variety of cell-cell signaling regulating for instance the development of the thymic epithelium.

Ephrin type-A receptor 4

EPHA4; TYRO1; CEK8; SEK1; RB; SEK; HEK8; AI385584; 2900005C20RIK

Q03137

Epha4; Sek; Sek1

Human Cells

A DNA sequence encoding the mouse EPHA4 (NP_031962.2) extracellular domain (Met 1-Thr 547) was as fused with the Fc region of human IgG1 at the C-terminus.

Mouse

The recombinant mouse EPHA4/Fc is a disulfide-linked homodimer. The reduced monomer consists of 768 amino acids and has a predicted molecular mass of 85.3 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rmEPHA4/Fc monomer is approximately 110 kDa due to glycosylation.

> 95 % as determined by SDS-PAGE

Measured by its binding ability in a functional ELISA. Immobilized mouse EPHA5 at 2 μg/ml (100 μl/well) can bind mouse EFNA4-Fc with a linear ranger of 1.28-32 ng/ml.