Recombinant Human EphB6 Protein (Fc Tag)(Active)
SKU: PKSH031775-100
Recombinant Human EphB6 Protein (Fc Tag)(Active)
SKU # | PKSH031775 |
Expression Host | HEK293 Cells |
Description
Synonyms | HEP |
Species | Human |
Expression Host | HEK293 Cells |
Sequence | Met 1-Ser 579 |
Accession | NP_004436.1 |
Calculated Molecular Weight | 86.5 kDa |
Observed Molecular Weight | 100-110 kDa |
Tag | C-hFc |
Bio-activity | 1. 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. 2. 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. |
Properties
Purity | > 90 % as determined by reducing SDS-PAGE. |
Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
Formulation | Lyophilized from sterile PBS, pH 7.4 Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
Reconstitution | Please refer to the printed manual for detailed information. |
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.