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Human EphB4 / HTK Protein

HTK,MYK1,TYRO11

Catalog Number P10235-HCCH
Organism Species Human
Host Human Cells
Synonyms HTK,MYK1,TYRO11
Molecular Weight The recombinant human EphB4 is a monomeric protein consisting of 530 amino acids and has a calculated molecular mass of 57.7 kDa. As a result of glycosylation, rhEphB4 migrates as an approximately 65-70 kDa protein in SDS-PAGE under reducing conditions.
predicted N Leu 16
SDS-PAGE
Purity > 95 % as determined by SDS-PAGE
Protein Construction The mature form of human EphB4 (NP_004435.3) extracellular domain (Met 1-Ala 539) with quinary-aa peptide (DDDDK) at the C-terminus was expressed and purified.
Bio-activity Measured by its binding ability in a functional ELISA . Immobilized human EphB4 at 2 μg/ml (100 μl/well) can bind human EphrinB2 with a linear range of 1-125 ng/ml .
Research Area Epigenetics |Transcription |Cancer susceptibility |Tumor Suppressor
Formulation Lyophilized from sterile 100mM NaCl, 50mM Tris, pH 7.5
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Ephrin type-B receptor 4 is a protein that in humans is encoded by the EPHB4 gene. It is a single-pass type I membrane protein belonging to the ephrin receptor subfamily of protein kinase superfamily. Members of the ephrin and Eph family are local mediators of cell function through largely contact-dependent processes in development and in maturity. Furthermore, EphB4 protein and the corresponding ligand Ephrin-B2 contribute to tumor growth in various human tumors. EphB4 protein has tumor suppressor activities and that regulation of cell proliferation, extracellular matrix remodeling, and invasive potential are important mechanisms of tumor suppression. Therefore, Ephrin-B2/EphB4 may be recognized as a novel prognostic indicator for cancers.
Reference
  • Davalos V, et al. (2006) EPHB4 and survival of colorectal cancer patients. Cancer Res. 66(18): 8943-8.
  • Zhao C, et al. (2006) Bidirectional ephrinB2-EphB4 signaling controls bone homeostasis. Cell Metab. 4(2): 111-21.
  • Kertesz N, et al. (2006) The soluble extracellular domain of EphB4 (sEphB4) antagonizes EphB4-EphrinB2 interaction, modulates angiogenesis, and inhibits tumor growth. Blood. 107(6): 2330-8.
  • Noren NK, et al. (2007) Paradoxes of the EphB4 receptor in cancer. Cancer Res. 67(9): 3994-7.
  • Taylor AC, et al. (2007) EphB4 expression along adult rat microvascular networks: EphB4 is more than a venous specific marker. Microcirculation. 14(3): 253-67.