Recombinant Human EphB2 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human EphB2 Fc Chimera is coated at 2 μg/mL, Recombinant Human Ephrin-B2 Fc Chimera
(Catalog # 7397-EB)
binds with an apparent Kd <0.1 nM.
Source
Mouse myeloma cell line, NS0-derived human EphB2 protein
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
84.7 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
103-108 kDa, reducing conditions
Publications
Read Publications using 5189-B2 in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 200 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human EphB2 Fc Chimera Protein, CF
CAPB
Cek5
Drt
DRTEphB2
EC 2.7.10
EC 2.7.10.1
EK5
elk-related tyrosine kinase
EPH receptor B2
eph tyrosine kinase 3
EphB2
EPH-like kinase 5
ephrin type-B receptor 2
EPHT3MGC87492
EPTH3
Erk
ERKHek5
Hek5
Nuk
PCBC
protein-tyrosine kinase HEK5
Qek2
Renal carcinoma antigen NY-REN-47
Sek3
Tyro5
Tyrosine-protein kinase receptor EPH-3
Tyrosine-protein kinase TYRO5
Background
EphB2, also known as Cek5, Nuk, Erk, Qek5, Tyro5, Sek3, Hek5, and Drt, is a 125 kDa member of the transmembrane Eph receptor tyrosine kinase family that binds members of the Ephrin family on adjacent cells. The interaction triggers forward signaling in the receptor-expressing cells through the Eph receptor and reverse signaling in the ligand-expressing cells through Ephrin (1, 2). Human EphB2 cDNA encodes a 1055 amino acid (aa) precursor, which includes an 18 aa signal sequence, a 525 aa extracellar domain (ECD), a 21 aa transmembrane segment, and a 491 aa cytoplamic domain. The ECD contains a cysteine-rich region followed by two fibronectin type III domains. The cytoplasmic domain contains the tyrosine kinase domain, a sterile alpha motif (SAM), and a PDZ binding motif (3). Human EphB2 shares 99% aa sequence identity with mouse and rat EphB2 within the ECD region. A short isoform that lacks 70 aa at the C-terminus has also been reported (4). Hippocampal neurons can release vesicles containing full length EphB2, and these are taken up by neighboring glial cells (5). EphB2 is expressed on both sides of the neuronal synapse. It controls axon guidance across the embryonic midline, promotes a neuronal fate from neural precursors, and regulates NMDA receptor activity (6-10). EphB2 interaction with Ephrin-A5 promotes axonal growth cone collapse, while its interaction with Ephrin-B ligands is required for inner ear, renal, urorectal, and vascular development (6, 11-15). Signaling in Ephrin expressing cells through EphB2-Ephrin complex requires proteolytic cleavage of EphB2 that releases its extracellular domain (16). Following the shedding of the extracellular domain of EphB2, the cytoplasmic domain of EphB2 is released from the plasma membrane by the presenilin-dependent gamma -secretase activity to initiate a signaling cascade in the EphB2 expressing cells (16). Aberrant EphB2 expression and activity are implicated in the progression of several cancers (17).
Pasquale, E.B. (2008) Cell 133:38.
Merlos-Suarez, A. and E. Batlle (2008) Curr. Opin. Cell Biol. 20:194.
Fox, G.M. et al. (1995) Oncogene 10:897.
Tang, X.X. et al. (1998) Oncogene, 17:521.
Lauterbach, J. and R. Klein (2006) J. Neurosci. 26:11575.
Cowan C.A. et al. (2000) Neuron 26:417.
Bouvier, D. et al. (2008) J. Neurochem. 106:682.
Cramer, K.S. et al. (2006) Dev. Biol. 295:76.
Katakowski, M. et al. (2005) Neurosci. Lett. 385:204.
Henderson, J.T. et al. (2001) Neuron 32:1041.
Himanen, J.-P. et al. (2004) Nat. Neurosci. 7:501.
Dravis, C. et al. (2007) Hear. Res. 223:93.
Dravis, C. et al. (2004) Dev. Biol. 271:272.
Ogawa, K. et al. (2006) J. Cell Sci. 119:559.
Salvucci, O. et al. (2006) Blood 108:2914.
Litterst, C. et al. (2007) J. Biol. Chem. 282:16155.
Castano, J. et al. (2008) Histol. Histopathol. 23:1011.
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