Recombinant Human EphB2 Protein (aa 570-987, His &GST Tag)(Active)
SKU: PKSH030383-50
Recombinant Human EphB2 Protein (aa 570-987, His &GST Tag)(Active)
SKU # | PKSH030383 |
Expression Host | Baculovirus-Insect Cells |
Description
Synonyms | CAPB, DRT, EK5, EPHB2, EPHT3, ERK, Ephrin type-B receptor 2, Hek5, PCBC, Tyro5 |
Species | Human |
Expression Host | Baculovirus-Insect Cells |
Sequence | Gly570-Val987 |
Accession | P29323-3 |
Calculated Molecular Weight | 75.2 kDa |
Observed Molecular Weight | 65 kDa |
Tag | N-His-GST |
Bio-activity | The specific activity was determined to be 120 nmol/min/mg using Poly(Glu:Tyr) 4:1 as substrate. |
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 | Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles. |
Shipping | This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at < - 20°C. |
Formulation | Supplied as sterile solution of 20mM Tris, 500mM NaCl, pH 7.4, 3mM DTT, 10% glycerol |
Reconstitution | Not Applicable |
Background
Ephrin type-B receptor 2; also known as EphB2; 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. EphB2 receptor tyrosine kinase phosphorylates syndecan-2 and that this phosphorylation event is crucial for syndecan-2 clustering and spine formation. 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.