|Datasheet||Specific References||Reviews||Related Products||Protocols|
|A DNA sequence encoding the cynomolgus EPHB6 (Met1-Ser591) was expressed, fused with the 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.
|> 85 % as determined by SDS-PAGE|
|1. Measured by its ability to bind human EFNB1-His (Cat:10894-H08H) in a functional ELISA.|
2. Immobilized EFNB2-His (Cat:10881-H08H) at 10 μg/ml (100 μl/well) can bind Cynomolgus EPHB6-Fc, The EC50 of Cynomolgus EPHB6-Fc is 20.6-48 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℃|
|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.
|The recombinant cynomolgus EPHB6 is a disulfide-linked homodimer. The reduced monomer comprises 801 amino acids and has a calculated molecular mass of 86.9 KDa.The apparent molecular mass of the protein is approximately 97 KDa respectively in SDS-PAGE.|
|Store it under sterile conditions at -70℃. 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.|
Ephrins are divided into the ephrin-A (EFNA) class and the ephrin-B (EFNB) class based on their structures and sequence relationships. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family. EphB6 is an unusual Eph receptor, lacking catalytic capacity due to alterations in its kinase domain. Interestingly, increased metastatic activity is associated with reduced EphB6 receptor expression in several tumor types, including breast cancer. This emphasizes the potential of EphB6 to act as a suppressor of cancer aggressiveness. EphB6 suppress cancer invasiveness through c-Cbl-dependent signaling, morphologic changes, and cell attachment and indicate that EphB6 may represent a useful prognostic marker and a promising target for therapeutic approaches. EphB6 can both positively and negatively regulate cell adhesion and migration, and suggest that tyrosine phosphorylation of the receptor by an Src family kinase acts as the molecular switch for the functional transition. In addition, Ephrin-B2 may be a physiological ligand for the EphB6 receptor.
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