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Recombinant Human EphA4 Protein (Fc Tag)
SKU: PKSH032385-50
Recombinant Human EphA4 Protein (Fc Tag)
| SKU # | PKSH032385 |
| Expression Host | HEK293 Cells |
Description
| Synonyms | EK8, EPH-like kinase 8, EPHA4, Ephrin type-A receptor 4, HEK8, SEK, TYRO1, Tyrosine-protein kinase TYRO1, Tyrosine-protein kinase receptor SEK, hEK8 |
| Species | Human |
| Expression Host | HEK293 Cells |
| Sequence | Val20-Thr547 |
| Accession | P54764 |
| Calculated Molecular Weight | 85.6 kDa |
| Observed Molecular Weight | 90-120 kDa |
| Tag | C-Fc |
| Bio-activity | Not validated for activity |
Properties
| Purity | > 95 % as determined by reducing SDS-PAGE. |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
| Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
| Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
| Formulation | Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, pH 8.0. Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
| Reconstitution | Please refer to the printed manual for detailed information. |
Background
Ephrin type-A receptor 4(EPHA4) belongs to the protein kinase superfamily and Ephrin receptor subfamily. EPHA4 contains 1 Eph LBD domain; 2 fibronectin type-III domains; 1 protein kinase domain and 1 SAM domain. EPH and EPH-related receptors have been implicated in mediating developmental events; particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands.