|Datasheet||Specific References||Reviews||Related Products||Protocols|
|EFNB2, RP11-272L14.1, EPLG5, HTKL, Htk-L, LERK5, MGC126226, MGC126227, MGC126228|
|A DNA sequence encoding the human EFNB2 (NP_004084.1) extracellular domain (Met 1-Ala 229) was was fused with the C-terminal polyhistidine-tagged Fc region of human IgG1 at the C-terminus.|
|In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.|
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
|> 97 % as determined by SDS-PAGE|
|Measured by its binding ability in a functional ELISA . Immobilized human EphB4-his at 2 μg/ml (100 μl/well) can bind human EphrinB2 Fc chimera with a linear range of 1-25 ng/ml . Immobilized human EphB4 at 2 μg/ml (100 μl/well) can bind human EphrinB2 Fc chimera with a linear range of 1-125 ng/ml.|
|< 1.0 EU per μg of the protein as determined by the LAL method|
|Samples are stable for up to twelve months from date of receipt at -70℃|
|The recombinant human EFNB2/Fc chimera is a disulfide-linked homodimeric protein. The reduced monomer consists of 450 amino acids and predicts a molecular mass of 50.3 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rh EFNB2/Fc monomer is approximately 62 kDa due to glycosylation.|
|Lyophilized from sterile PBS, pH 7.4|
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
|Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.|
|A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.|
EphrinB2 also known as EFNB2 is a member of the ephrin family. EphrinB2 is involved in establishing arterial versus venous identity and perhaps in anastamosing arterial and venous vessels at their junctions. The transmembrane-associated ephrin ligands and their Eph family of receptor tyrosine kinases are expressed by cells of the SVZ. Eph/ephrin interactions are implicated in axon guidance, neural crest cell migration, establishment of segmental boundaries, and formation of angiogenic capillary plexi. Eph receptors and ephrins are divided into two subclasses, A and B, based on binding specificities. Ephrin subclasses are further distinguished by their mode of attachment to the plasma membrane: ephrin-A ligands bind EphA receptors and are anchored to the plasma membrane via a glycosylphosphatidylinositol (GPI) linkage, whereas ephrin-B ligands bind EphB receptors and are anchored via a transmembrane domain. An exception is the EphA4 receptor, which binds both subclasses of ephrins. EphrinB2 expression progressively extends from the arterial endothelium to surrounding smooth muscle cells and to pericytes, suggesting that ephrin-B2 may play an important role during formation of the arterial muscle wall.