EphB4 / HTK Protein

EPH Receptor B4 / EphB4 Protein

EphB4 Protein Product Information

• EphB4 Synonym: EphB4, HTK, MYK1, TYRO11
• 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.
• Source: Human
• Expression Host: Human Cells

EphB4 Protein QC Testing

• Purity: > 95 % as determined by SDS-PAGE
• 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
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Leu 16
• Molecular Mass: 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.
• Formulation: Lyophilized from sterile 100mM NaCl, 50mM Tris, pH 7.5
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: EphB4 protein

EphB4 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage and usage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

EphB4 Protein Description

EphB4, also known as Htk, Myk-1, is a member of the Eph subfamily of receptor tyrosine kinases (RTKs). The Ephs are divided into two classes based on their extracellular structure and ligand specificity, and the transmembrane receptor binding preferentially to ephrin-B ligands is referred to as EphB. Sharing common structure organization, all Eph receptors contain an N-terminal Ig-like domain, a cysteine-rich region and two fibronectin type I II domains within the ECD, as well as the typical cytoplasmic tyrosine kinase domain. EphB4 and its ligand ephrin-B2 are specifically expressed on venous and arterial endothelial cells, respectively, and play an essential role in vascular development via bidirectional signals. The forward EphB4 signaling inhibits cell adhesion, chemotaxis, angiogenesis, and tumor growth. In contrast, the reverse Ephrin-B2 signaling exerts the opposite effect. It has been reported that aberrant expression of EphB4 is associated with prostate cancer and highly malignant breast cancers, and accordingly, EphB4 has potential applications as a therapeutic candidate.

References

1. Bennett, B.D. et al., 1994, J. Biol. Chem. 269: 14211-14218.
2. Noren, N.K. et al., 2004, Proc. Natl. Acad. Sci. 101: 5583-5588.
3. Murai, K.K. et al., 2003, J. Cell. Sci. 116: 2823-2832.
4. Noren, N.K. et al., 2006, Nat. Cell. Biol. 8: 815-825.
5. Xia, G. et al., 2005, Cancer Res. 65: 4623-4632.
6. Kertesz, N. et al., 2006, Blood. 107: 2330-2338.