Recombinant Mouse EphA4 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized Recombinant Mouse EphA4 Fc Chimera at 2 µg/mL (100 µL/well) can bind recombinant human Ephrin-A5 Fc Chimera with a linear range of 0.16-10 ng/mL. Optimal dilutions should be determined by each laboratory for each application.
Source
Mouse myeloma cell line, NS0-derived mouse EphA4 protein
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
85.7 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 641-A4 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 MES, NaCl, CHAPS, Imidazole and PEG 3350.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 400 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 EphA4 Fc Chimera Protein, CF
Cek8
EC 2.7.10
EC 2.7.10.1
EK8
EPH receptor A4
EphA4
EPH-like kinase 8
ephrin type-A receptor 4
Hek8
receptor protein-tyrosine kinase HEK8
SEK
Sek1
TYRO1 protein tyrosine kinase
Tyro1
Tyrosine-protein kinase receptor SEK
Tyrosine-protein kinase TYRO1
Background
EphA4, also known as Hek8, Tyro1, and Sek, is a 120‑130 kDa glycosylated member of the Eph family of transmembrane receptor tyrosine kinases (1, 2). The A and B classes of Eph proteins are distinguished by Ephrin ligand binding preference but have a common structural organization. EphA4 is unusual in its ability to be activated by both Ephrin-A and -B molecules, although its interactions with Ephrin-B2 and -B3 are weaker than with Ephrin-A ligands (3, 4). Eph-Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression. The 528 amino acid (aa) extracellular domain (ECD) of mouse EphA4 contains an N-terminal Ephrin binding region, a cysteine-rich region, and two fibronectin type III domains (FnIII). The 417 aa cytoplasmic domain contains the tyrosine kinase domain and a sterile alpha motif (SAM) (5). Within the ECD, mouse EphA4 shares 98.3% and 99.6% aa sequence identity with human and rat EphA4, respectively. Alternate splicing of mouse EphA4 generates a short isoform with a 50 aa deletion within the kinase domain. EphA4 is activated by interactions with Ephrin ligands, triggering a repulsive effect on neurite migration (6, 7). This function is important for the accurate guidance and pathfinding of neurites and axons in the spiral ganglion of the cochlea, the anterior commissure, and the corticospinal tract (6‑8). Neuronal EphA4 interactions with astrocyte‑expressed Ephrins also plays a critical role in long term potentiation by regulating hippocampal neuron dendrite arborization, spine maturation, and function (9‑11). The up‑regulation of EphA4 in gastric carcinoma is negatively correlated with patient survival (12). In glioma, EphA4 associates with FGF R1, and this enhances FGF basic-induced tumor cell migration (13). EphA4 is also involved in morphogenesis of the thymic epithelium and T cell development (14).
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