Recombinant Mouse EphA3 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized rmEphA3/Fc Chimera at 2 µg/mL (100 µL/well) can bind rhEphrin A5 Fc Chimera with a linear range of 0.08-5 ng/mL. Optimal dilutions should be determined by each laboratory for each application.
Source
Mouse myeloma cell line, NS0-derived mouse EphA3 protein
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
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.
SDS-PAGE
110 kDa, reducing conditions
Publications
Read Publications using 640-A3 in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Tris.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse EphA3 Fc Chimera Protein, CF
Cek4
EC 2.7.10
EC 2.7.10.1
EK4
EPH receptor A3
EphA3
EPH-like kinase 4
ephrin type-A receptor 3
ETK
Hek4
HEKETK1eph-like tyrosine kinase 1
human embryo kinase 1
TYRO4 protein tyrosine kinase
Tyro4
Tyrosine-protein kinase receptor ETK1
Tyrosine-protein kinase TYRO4
Background
EphA3, also known as Cek4, Mek4, Hek, Tyro4, and Hek4, is a 135 kDa glycosylated member of the transmembrane Eph receptor tyrosine kinase family. The A and B classes of Eph proteins are distinguished by Ephrin ligand binding preference but have a common structural organization. EphA3 preferentially binds to Ephrin-A5. Eph-Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression (1, 2). The 520 amino acid (aa) extracellular domain (ECD) of mouse EphA3 contains an N-terminal Ephrin binding region, a cysteine-rich region, and two fibronectin type II domains. The 419 aa cytoplasmic domain contains the tyrosine kinase domain and a sterile alpha motif (SAM) (3, 4). Within the ECD, mouse EphA3 shares 96% and 98% aa sequence identity with human and rat EphA3, respectively. Alternate splicing generates a secreted isoform that consists of nearly the entire ECD. EphA3 is expressed in the developing forebrain, retinal axons, some spinal cord motor neurons, and the heart where it plays an important role in axonal repulsion and organ morphogenesis (5 ‑ 8). It is upregulated on some hematopoietic and solid tumor cells and on astrocytes surrounding injured nervous tissue (5, 9 - 11). EphA3 ligation inhibits cellular adhesion to fibronectin as well as cellular migration (9, 10). Transmembrane EphA3 associates in cis with ADAM10 which then promotes the cleavage in trans of Ephrin-A5 (12). It also associates in cis with Ephrin-A5 on retinal axons, thereby preventing the activation of EphA3 by Ephrin-A (13). Multiple tyrosine residues within the cytoplasmic region of EphA3 become phosphorylated during ligand-induced signaling (14, 15).
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