Recombinant Mouse EphB2 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized rmEphB2/Fc Chimera at 2 µg/mL (100 µL/well) can bind rmEphrin-B2/Fc Chimera with a linear range of 0.039-2.5 ng/mL.
Source
Mouse myeloma cell line, NS0-derived mouse 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
85.3 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
100-110 kDa, reducing conditions
Publications
Read Publications using 467-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 Tris.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 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 Mouse 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, Qek2, Tyro5, Sek3, Hek5, and Drt (1), is a member of the Eph receptor family which binds members of the ephrin ligand family. There are two classes of receptors, designated A and B. Both the A and B class receptors have an extracellular region consisting of a globular domain, a cysteine-rich domain, and two fibronectin type III domains. This is followed by the transmembrane region and the cytoplasmic region. The cytoplasmic region contains a juxtamembrane motif with two tyrosine residues which are the major autophosphorylation sites, a kinase domain, and a conserved sterile alpha motif (SAM) in the carboxy tail which contains one conserved tyrosine residue. Activation of kinase activity occurs after ligand recognition and binding. EphB2 has been shown to bind ephrin-B1, ephrin-B2, and ephrin-B3 (2, 3). The extracellular domains of human and mouse EphB2 share 99% amino acid identity. Only membrane-bound or Fc-clustered ligands are capable of activating the receptor in vitro. Soluble monomeric ligands bind the receptor but do not induce receptor autophosphorylation and activation (2). In vivo, the ligands and receptors display reciprocal expression (3). It has been found that nearly all the receptors and ligands are expressed in developing and adult neural tissue (3). The ephrin/Eph families also appear to play a role in angiogenesis (3).
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