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Recombinant Human Ephrin-A4/EFNA4 Protein (His Tag)
SKU: PKSH032391-50
Recombinant Human Ephrin-A4/EFNA4 Protein (His Tag)
| SKU # | PKSH032391 |
| Expression Host | HEK293 Cells |
Description
| Synonyms | EFNA4, EPH-Related Receptor Tyrosine Kinase Ligand 4, EPLG4, Ephrin-A4, LERK-4, LERK4 |
| Species | Human |
| Expression Host | HEK293 Cells |
| Sequence | Leu26-Gly171 |
| Accession | P52798 |
| Calculated Molecular Weight | 17.4 kDa |
| Observed Molecular Weight | 20 kDa |
| Tag | C-His |
| Bio-activity | Not validated for activity |
Properties
| Purity | > 90 % 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 PBS, 5% Trehalose, 5% Mannitol, 0.01% Tween 80, pH7.4. 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-A4 is a member of the ephrin ligand family which binds members of the Eph receptor family. All ligands share a conserved extracellular sequence; which most likely corresponds to the receptor binding domain. Ephrin-A4 consists of approximately 125 amino acids and includes four invariant cysteines; It has been shown to bind EphA2; EphA3; EphA4; EphA5; EphA6; EphA7; and EphB1. Ephrin-A4 binds promiscuously Eph receptors residing on adjacent cells; leading to contact-dependent bidirectional signaling into neighboring cells. It may play a role in the interaction between activated B-lymphocytes and dendritic cells in tonsils.