Name :
Recombinant Human EphB6 Protein (hFc Tag)

Biological Activity :

Background :
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.

Biological Activity :
1. Measured by its binding ability in a functional ELISA.2. Immobilized recombinant human EphrinB1 at 10 μg/ml (100 μl/well) can bind human EphB6 with a linear range of 0.16-4 μg/ml.3. Immobilized recombinant human EphrinB2 at 10 μg/ml (100 μl/well) can bind human EphB6 with a linear range of 1.28-32 ng/ml.

Expression Host :
Human

Source :
HEK293 Cells

Tag :

Protein Accession No. :
NP_004436.1

NCBI Gene ID :

Synonyms :

Synonyms :
EPH receptor B6

Amino Acid Sequence :

Molecular Weight :
The recombinant mature human EphB6/Fc chimera is a disulfide linked homodimeric protein. Each monomer consists of 801 amino acids and has a calculated molecular mass of 86.5 kDa. In SDS-PAGE under reducing conditions, rhEphB6/Fc monomer migrates with an apparent molecular mass of approximately 100-110 kDa due to glycosylation.

Purity :
> 90 % as determined by SDS-PAGE

State of Matter :

Product Concentration :

Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. 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.

Endotoxin Level :
< 1.0 EU per μg of the protein as determined by the LAL method

Protein Construction :
The extracellular domain (Met 1-Ser 579) of human EphB6 (NP_004436.1) precursor was fused with the Fc region of human IgG1 at the C-terminus.

Buffer Solution :
Lyophilized from sterile PBS, pH 7.4.Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.

Shipping :
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.

Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.

Synonyms :
EPHB5 Protein, Human; HEP Protein, Human EphB6 背景信息 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.

References & Citations :
Munthe E, et al. (2000)Ephrin-B2 is a candidate ligand for the Eph receptor, EphB6. FEBS Lett. 466(1): 169-74.Matsuoka H, et al. (2005) Biphasic functions of the kinase-defective EphB6 receptor in cell adhesion and migration. J Biol Chem. 280(32): 29355-63.Truitt L, et al. (2010) The EphB6 receptor cooperates with c-Cbl to regulate the behavior of breast cancer cells. Cancer Res. 70(3): 1141-53.

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