Recombinant Mouse EphA7 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized recombinant mouse EphA7 Fc Chimera at 2 µg/mL (100 µL/well) can bind recombinant human Ephrin-A4 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 EphA7 protein
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 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 608-A7 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 PBS.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
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 EphA7 Fc Chimera Protein, CF
Cek11
Ebk
EC 2.7.10
EC 2.7.10.1
Ehk3
EHK-3
EK11
EPH homology kinase 3
Eph homology kinase-3
EPH receptor A7
EphA7
EPH-like kinase 11
ephrin type-A receptor 7
Hek11
Mdk1
receptor protein-tyrosine kinase HEK11
tyrosine-protein kinase receptor EHK-3
Background
EphA7, also known as Mdk1, Hek11, Ehk3, Ebk, and Cek11, is a 115-120 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. EphA7 preferentially binds to and is activated by Ephrin-A1, -A2, -A3, -A4, and -A5 (3 - 6). Eph-Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression. The 527 amino acid (aa) extracellular domain (ECD) of mouse EphA7 contains an N‑terminal Ephrin binding region, a cysteine-rich region, and two fibronectin type III domains (FnIII). The 421 aa cytoplasmic domain contains the tyrosine kinase domain and a sterile alpha motif (SAM) (7). Within the ECD, mouse EphA7 shares 98% and 99% aa sequence identity with human and rat EphA7, respectively. Alternate splicing generates a differentially expressed kinase-defective isoform of mouse EphA7 that lack most of the cytoplasmic domain and a soluble isoform that is truncated following the first FnIII domain (4, 6 - 9). In mouse, EphA7 is expressed in discrete regions of the developing and adult neocortex (4, 7 - 10), Purkinje layer of the cerebellum (7), limbic system (4, 8 ‑ 10), visual and auditory systems (7, 8, 11), and the peripheral sensory nervous system (7, 8). EphA7 functions as a repulsive guidance molecule during the targeting of retinal axons to the superior colliculus and of neocortical axons to the thalamus (4, 10, 11). EphA7 is also expressed in mesenchymal cells along routes of axon innervation during limb development (12). EphA7 ligands are expressed in a complementary pattern during embryogenesis (3, 10 - 12). EphA7 is selectively expressed in early stages of the B cell lineage, and a 50 kDa secreted form is produced by mature peripheral B and T cells (6, 13). This isoform is also expressed in human lung carcinoma (14). EphA7 can be up or downregulated in a variety of human cancers (6, 15, 16).
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