Human EphB6/Eph Receptor B6 recombinant protein

Human EphB6/Eph Receptor B6 recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

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.

MGC129911; HEP; MEP; CEKL; EPHB6; MGC129910

O15197

Human Cells

The mature form of human EphB6 (NP_004436.1) extracellular domain (Met 1-Ser 579) with quinary-aa peptide (DDDDK) at the C-terminus was expressed and purified.

Human

The recombinant mature human EphB6 consists of 569 amino acids and has a calculated molecular mass of 60.4 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhEphB6 is approximately 72 kDa due to glycosylation.

> 95 % as determined by SDS-PAGE and SEC-HPLC Analysis.

Measured by its binding ability in a functional ELISA.
Immobilized human EphB6 (Cat:504530) at 10 μg/mL (100 μl/well) can bind biotinylated human EFNB2-Fch (Cat:502066) with a linear range of 1.56-50 ng/mL.