Recombinant Human EphA8 Fc Chimera Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human EphA8 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human EphA8 Fc Chimera is coated at 2 μg/mL (100 μL/well), the concentration of Biotinylayed Recombinant Human Ephrin-A5 Fc Chimera (Catalog # BT374) that produces 50% of the optimal binding response is 2-12 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human EphA8 protein
Human EphA8
(Glu31-Thr542)
Accession # NP_065387
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Glu31
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
EPHA8
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
83.2 kDa (monomer).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
94 kDa, reducing conditions
Publications
Read Publication using
6828-A8 in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after opening.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in MES, NaCl, PEG, CHAPS and Imidazole.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human EphA8 Fc Chimera Protein, CF

  • Eek
  • EK3
  • EPH- and ELK-related kinase
  • EPH- and ELK-related tyrosine kinase
  • EPH receptor A8
  • EphA8
  • EPH-like kinase 3
  • ephrin type-A receptor 8
  • Hek3
  • hydroxyaryl-protein kinase
  • KIAA1459
  • protein-tyrosine kinase
  • tyrosine-protein kinase receptor EEK
  • tyrosylprotein kinase

Background

EphA8, also known as Hek3 and Eek, is a 120 kDa glycosylated member of the Eph family of transmembrane receptor tyrosine kinases (1, 2). The A and B classes of Eph proteins are distinguished by Ephrin ligand binding preference but have a common structural organization. EphA4 binds and is activated by class A Ephrins but not class B Ephrins (3, 4). Eph-Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression. The 512 amino acid (aa) extracellular domain (ECD) of human EphA8 contains an N-terminal Ephrin binding region, a cysteine-rich region, and two fibronectin type III domains (FnIII). The 442 aa cytoplasmic domain contains the tyrosine kinase domain and a sterile alpha motif (SAM) (5). Within the ECD, human EphA8 shares 97% aa sequence identity with mouse and rat EphA8. EphA8 is expressed in neurons in the mesencephalon of the developing brain, particularly in the rostral tectum and the superior colliculus (6-8). It is enriched at the tips of neurite processes and plays a role in projection of superior colliculus axons through the posterior commissure (7, 9). Its expression enhances neurite extension by means of a mechanism that does not require catalytic activity of the tyrosine kinase domain (10). Ephrin-mediated activation of the EphA8 kinase induces phosphorylation of tyrosine residues in the cytoplasmic domain, leading to association with signaling and scaffolding proteins and inhibition of cell-cell adhesion (4, 9, 11). Ligand binding can also promote the Integrin-mediated cellular adhesion to Fibronectin (12). This function, like the enhancement of neurite extension, does not require activation of the kinase domain (12).
  1. Pasquale, E.B. (2005) Nat. Rev. Mol. Cell Biol. 6:462.
  2. Merlos-Suarez, A. and E. Batlle (2008) Curr. Opin. Cell Biol. 20:194.
  3. Park, S. and M.P. Sanchez (1997) Oncogene 14:533.
  4. Choi, S. et al. (1999) Mol. Cells 9:440.
  5. Chan, J. and V.M. Watt (1991) Oncogene 6:1057.
  6. Koo, J. et al. (2003) Dev. Dyn. 226:596.
  7. Park, S. et al. (1997) EMBO J. 16:3106.
  8. Shim, S. et al. (2007) Mol. Cell. Biol. 27:1614.
  9. Shin, J. et al. (2007) Mol. Cell. Biol. 27:8113.
  10. Gu, C. et al. (2005) Oncogene 24:4243.
  11. Choi, S. and S. Park (1999) Oncogene 18:5413.
  12. Gu, C. and S. Park (2001) Mol. Cell. Biol. 21:4579.

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Publications for EphA8 (6828-A8)(1)

We have publications tested in 1 confirmed species: N/A.

We have publications tested in 1 application: ELISA Capture.


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Bioinformatics

Gene Symbol EPHA8
Uniprot