Rat EphA4 Protein (Fc Tag)
EPHA4
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Catalog Number | P80123-R02H |
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Organism Species | Rat |
Host | Human Cells |
Synonyms | EPHA4 |
Molecular Weight | The recombinant rat EPHA4/Fc is a disulfide-linked homodimer. The reduced monomer comprises 769 amino acids and has a predicted molecular mass of 85.3 kDa. The apparent molecular mass of the protein is approximately 98 kDa in SDS-PAGE under reducing conditions. |
predicted N | Val 20 |
SDS-PAGE | |
Purity | > 98 % as determined by SDS-PAGE |
Protein Construction | A DNA sequence encoding the rat EPHA4 (D3ZZK3) (Met1-Tyr547) was expressed, fused with the Fc region of human IgG1 at the C-terminus. |
Bio-activity | Measured by its binding ability in a functional ELISA. Immobilized mouse EFNA5-His (P50597-M08H) at 10 μg/ml (100 μl/well) can bind Rat EPHA4-Fc, The EC50 of Rat EPHA4-Fc is 19.8-46.3 ng/ml. |
Research Area | Signaling |Signal Transduction |Receptor Tyrosine Kinases (RTKs) |
Formulation | Lyophilized from sterile PBS, pH 7.4 1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. |
Background | EPH receptor A4 (ephrin type-A receptor 4), also known as EphA4, belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family which 16 known receptors (14 found in mammals) are involved: EPHA1, EPHA2, EPHA3, EPHA4, EPHA5, EPHA6, EPHA7, EPHA8, EPHA9, EPHA10, EPHB1, EPHB2, EPHB3, EPHB4, EPHB5, EPHB6. The Eph family of receptor tyrosine kinases (comprising EphA and EphB receptors) has been implicated in synapse formation and the regulation of synaptic function and plasticity6. EphA4 is enriched on dendritic spines of pyramidal neurons in the adult mouse hippocampus, and ephrin-A3 is localized on astrocytic processes that envelop spines. Eph receptor−mediated signaling, which is triggered by ephrins7, probably modifies the properties of synapses during synaptic activation and remodeling. Ephrin receptors are components of cell signalling pathways involved in animal growth and development, forming the largest sub-family of receptor tyrosine kinases (RTKs). The extracellular domain of an EphA4 interacts with ephrin ligands, which may be tethered to neighbouring cells. Ligand-mediated activation of Ephs induce various important downstream effects and Eph receptors have been studied for their potential roles in the development of cancer. |
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