Human EphB3 / HEK2 Protein (aa 585-998, His & GST Tag)
ETK2,HEK2,TYRO6
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| Catalog Number | P13925-H20B1 |
|---|---|
| Organism Species | Human |
| Host | Baculovirus-Insect Cells |
| Synonyms | ETK2,HEK2,TYRO6 |
| Molecular Weight | The recombinant human EPHB3 /GST chimera consists of 651 amino acids and has a calculated molecular mass of 74.7 kDa. The recombinant protein migrates as an approximately 64 kDa band in SDS-PAGE under reducing conditions. |
| predicted N | Met |
| SDS-PAGE |  |
| Purity | > 90 % as determined by SDS-PAGE |
| Protein Construction | A DNA sequence encoding the human EPHB3 (P54753) (Gln585-Val998) was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus. |
| Bio-activity | The specific activity was determined to be 90 nmol/min/mg using Poly(Glu:Tyr) 4:1 as substrate. |
| Research Area | Cardiovascular |Angiogenesis |Growth Factor & Receptor |Ephrin & Eph Receptor |Eph Receptor |
| Formulation | Supplied as sterile 20mM Tris, 500mM NaCl, pH 7.4, 10% gly 1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. |
| Background | Ephrin type-B receptor 3, also known as EphB3 or HEK2, 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. Ephrin receptors are components of cell signalling pathways involved in animal growth and development, forming the largest sub-family of receptor tyrosine kinases (RTKs). 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. EphB receptor tyrosine kinases are enriched at synapses, suggesting that these receptors play a role in synapse formation or function. We find that EphrinB binding to EphB induces a direct interaction of EphB with NMDA-type glutamate receptors. This interaction occurs at the cell surface and is mediated by the extracellular regions of the two receptors, but does not require the kinase activity of EphB. |
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