• Purity

  >90%, by SDS-PAGE under reducing conditions and visualized by silver stain.

• Endotoxin Level

  <0.10 EU per 1 μg of the protein by the LAL method.  

• Activity

  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 (Val27-Lys548) Accession # P54763	DIEGRMD	Human IgG1 (Pro100-Lys330)	6-His tag
  N-terminus			C-terminus

• Accession #

• N-terminal Sequence    
  Analysis

  Val27

• Structure / Form

  Disulfide-linked homodimer

• Predicted Molecular Mass

  85.3 kDa (monomer)

• SDS-PAGE

  100-110 kDa, reducing conditions

Background: EphB2

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).

• References:

1. Eph Nomenclature Committee [letter] (1997) Cell 90:403.

2. Flanagan, J.G. and P. Vanderhaeghen (1998) Annu. Rev. Neurosci. 21:309.

3. Pasquale, E.B. (1997) Curr. Opin. Cell Biol. 9:608.

• Long Name:

  Eph Receptor B2

• Entrez Gene IDs:

  2048 (Human); 13844 (Mouse)

• Alternate Names:

  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