Cynomolgus EphB6 / EphB6 Protein (Fc Tag)

EPHB6

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Catalog Number	P90045-C02H
Organism Species	Cynomolgus
Host	Human Cells
Synonyms	EPHB6
Molecular Weight	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.
predicted N	Leu 32
SDS-PAGE
Purity	> 85 % as determined by SDS-PAGE
Protein Construction	A DNA sequence encoding the cynomolgus EPHB6 (Met1-Ser591) was expressed, fused with the Fc region of human IgG1 at the C-terminus.
Bio-activity	1. Measured by its ability to bind human EFNB1-His (P10894-H08H) in a functional ELISA. 2. Immobilized EFNB2-His (P10881-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.
Research Area	Signaling \|Signal Transduction \|Growth Factor & Receptor \|Ephrin & Eph Receptor \|Eph Receptor
Formulation	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.
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.
Reference	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.