EphB6 Proteins, Antibodies, cDNA Clones, ELISA Kits Research Reagents

All EphB6 reagents are produced in house and quality controlled, including 9 EphB6 Antibody, 2 EphB6 ELISA, 40 EphB6 Gene, 5 EphB6 Lysate, 5 EphB6 Protein, 2 EphB6 qPCR. All EphB6 reagents are ready to use.

EphB6 Protein (5)

    EphB6 Antibody (9)

      EphB6 ELISA Kit & Match Antibody ELISA Pair Set (2)

      EphB6 cDNA Clone (40)

      NM_004445.2
      NM_001146351.1
      NM_001107857.1
      XM_001089756.2

      In cloning vector

      EphB6 qPCR Primer (2)

      EphB6 Lysate (5)

        EphB6 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.

        EphB6 References

        • 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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