Reactivity | MuSpecies Glossary |
Applications | Binding Activity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. Immobilized rmEphA6/Fc Chimera at 2 µg/mL (100 µL/well) can bind rhEphrin-A3/Fc Chimera with a linear range of 0.31-20 ng/mL. Optimal dilutions should be determined by each laboratory for each application. |
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Source | Mouse myeloma cell line, NS0-derived mouse EphA6 protein
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Accession # | |||||||||
N-terminal Sequence | Ser28 |
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Structure / Form | Disulfide-linked homodimer |
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Protein/Peptide Type | Recombinant Proteins |
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Gene | Epha6 |
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Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
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Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 86 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 100 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in MES, NaCl, PEG 3350, CHAPS and Imidazole. |
Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
EphA6, also known as Ehk2 and Hek12 (1), is a member of the Eph receptor family which binds members of the ephrin ligand family. There are two classes of receptors, designated A and B. Both the A and B class receptors have an extracellular region consisting of a globular domain, a cysteine-rich domain, and two fibronectin type III domains. This is followed by the transmembrane region and cytoplasmic region. The cytoplasmic region contains a juxtamembrane motif with two tyrosine residues, which are the major autophosphorylation sites, a kinase domain, and a conserved sterile alpha motif (SAM) in the carboxy tail which contains one conserved tyrosine residue. Activation of kinase activity occurs after ligand recognition and binding. EphA6 has been shown to bind ephrin-A2, ephrin-A1, ephrin-A3, ephrin-A4, and ephrin-A5 (2, 3). The extracellular domains of rat and mouse EphA6 share 99% amino acid identity. Only membrane-bound or Fc-clustered ligands are capable of activating the receptor in vitro. While soluble monomeric ligands bind the receptor, they do not induce receptor autophosphorylation and activation (2). In vivo, the ligands and receptors display reciprocal expression (3). It has been found that nearly all receptors and ligands are expressed in developing and adult neural tissue (3). The Eph/ephrin families also appear to play a role in angiogenesis (3).
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