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Human EphA3 Protein (His Tag)

EK4,ETK,ETK1,HEK,HEK4,TYRO4

Catalog Number P11459-H08H
Organism Species Human
Host Human Cells
Synonyms EK4,ETK,ETK1,HEK,HEK4,TYRO4
Molecular Weight The recombinant human EPHA3 consists of 532 amino acids and predicts a molecular mass of 60.3 KDa. It migrates as an approximately 65-70 KDa band in SDS-PAGE under reducing conditions.
predicted N Glu 21
SDS-PAGE
Purity > 95 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human EPHA3 (Met1-Gln541) was expressed with a polyhistidine tag at the C-terminus.
Bio-activity Measured by its binding ability in a functional ELISA.
Immobilized human EPHA3-His at 10 μg/ml (100 μl/well) can bind human EphrinA5-Fc (P10192-H02H), The EC50 of human EphrinA5-Fc (P10192-H02H) is 6.2-14.6 ng/ml.
Research Area Cancer |Invasion microenvironment |Angiogenesis |Eph Receptors
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 EPHA3 gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. 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. EPHA3 gene encodes a protein that binds ephrin-A ligands. EPHA3 is involved in the retinotectal mapping of neurons. It may also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development.
Reference
  • Holder N, et al. (1999) Eph receptors and ephrins: effectors of morphogenesis. Development. 126(10):2033-44.
  • Wilkinson DG. (2000) Eph receptors and ephrins: regulators of guidance and assembly. Int Rev Cytol. 196:177-244.
  • Xu Q, et al. (2001) Roles of Eph receptors and ephrins in segmental patterning. Philos Trans R Soc Lond B Biol Sci. 355(1399):993-1002.