EphA6/Fc Chimera from mouse

EphA6 (ephrin receptor A6) is a receptor tyrosine kinase (RTK), which belongs to a 16 member family of ephrin receptors. This family is divided into two classes A and B. EphA5 belongs to EphA group, which contains 10 members. The ligands to this group of receptors are glycosylphosphatidylinositol (GPI)-anchored named ephrin-A1-A6. The members of this family have an ephrin-binding domain in its N-terminal globular domain, succeeded by a linker region rich in cysteine and two fibronectin type III repeats in the exoplasmic domain. Its cytoplasmic domain consists of a juxtamembrane region, a conserved tyrosine kinase domain, an α-helical C-terminal domain, and a PDZ domain-binding domian.

EphA6 (ephrin receptor A6) is a frequently mutated gene in colorectal cancer, in African-American population. In developing human retina, it is found in the ganglion cells of macula. It is involved in repellant-signaling, and hence, is involved in vascular patterning of retina, and also maintaining postnatal projection from ganglion cells of macula and fovea.

Member of the Eph receptor tyrosine kinase family shown to bind ephrin-A1, ephrin-A2, ephrin-A3, ephrin-A4, and ephrin-A5; involved in pattern formation and morphogenesis.

Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline.

The biological activity is measured by its ability to bind recombinant human ephrin-A3/Fc in an ELISA assay.

Extracellular domain of mouse EphA6 (amino acids 1-546) fused by means of a polypeptide linker to the Fc region of human IgG1 that is histidine-tagged at the C-terminus.