Recombinant Human EphB6 Fc Chimera Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

Order Details

Recombinant Human EphB6 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized rhEphB6/Fc Chimera at 2 µg/mL (100 µL/well) can bind rmEphrin-B2/Fc Chimera with a linear range of 0.0780-5.00 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human EphB6 protein
Human EphB6
(Leu17-Ser579)
Accession #AAI10608.2
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Leu17
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
EPHB6
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Binding Activity
Theoretical MW
86.7 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
104 kDa, under reducing conditions.
Publications
Read Publication using
3384-B6 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, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Human EphB6 Fc Chimera Protein, CF

  • EC 2.7.10.1
  • EPH receptor B6
  • EphB6
  • ephrin type-B receptor 6
  • Hep
  • HEPTyrosine-protein kinase-defective receptor EPH-6
  • Mep
  • MGC129910
  • MGC129911

Background

EphB6, also known as Hep and Mep, is a 110 kDa member of the Eph receptor tyrosine kinase family. The A and B classes of Eph proteins are distinguished by ligand preference and have a common structural organization (1 - 4). The human EphB6 cDNA encodes a 1006 amino acid (aa) precursor that includes a 16 aa signal sequence, a 563 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 406 aa cytoplasmic domain. The ECD contains serine- and cysteine-rich regions and two fibronectin type-III domains. The cytoplasmic domain contains one non-catalytic protein kinase-like, one proline-rich, one SAM, and one PDZ-binding domain (5, 6). Within the ECD, human EphB6 shares 91% aa sequence identity with mouse and rat EphB6. It shares 38 - 45% aa sequence identity with human EphB1, 2, 3, 4, and 6. Human EphB5 has not been characterized. Two secreted splice variants have been described in mouse but not in human (6). EphB6 is primarily expressed in brain, pancreas, thymus, and peripheral T cells (5, 7, 8). EphB6 forms stable heterodimers with EphB1 and participates in signal transduction by association with other enzymatically active molecules (9 - 11). Ephrin-B2 is the dominant ligand for EphB6, although Ephrin-B1 and Ephrin-B3 can also trigger responses (12 - 14). High concentrations of Ephrin-B2 inhibit cell adhesion and migration as well as tyrosine phosphorylation of EphB6. Conversely, low concentrations of Ephrin-B2 promote adhesion and migration and do not lead to EphB6 phosphorylation (15). The level of EphB6 expression is inversely correlated with tumor aggressiveness in a variety of malignancies (1). EphB6 also functions as a T cell co-stimulatory molecule (8, 11, 13). EphB6 clusters with the T cell receptor and participates in the subsequent attenuation of the T cell response (8, 10, 11, 13).

  1. Surawska, H. et al. (2004) Cytokine Growth Factor Rev. 15:419.
  2. Poliakov, A. et al. (2004) Dev. Cell 7:465.
  3. Wu, J. and H. Luo (2005) Curr. Opin. Hematol. 12:292.
  4. Pasquale, E.B. (2005) Nat. Rev. Mol. Cell Biol. 6:462.
  5. Matsuoka, H. et al. (1997) Biochem. Biophys. Res. Commun. 235:487.
  6. Gurniak, C.B. and L.J. Berg (1996) Oncogene 13:777.
  7. Hafner, C. et al. (2004) Clin. Chem. 50:490.
  8. Luo, H. et al. (2002) J. Clin. Invest. 110:1141.
  9. Freywald, A. et al. (2002) J. Biol. Chem. 277:3823.
  10. Freywald, A. et al. (2003) J. Biol. Chem. 278:10150.
  11. Luo, H. et al. (2001) J. Immunol. 167:1362.
  12. Munthe, E. et al. (2000) FEBS Lett. 466:169.
  13. Luo, H. et al. (2004) J. Clin. Invest. 114:1762.
  14. Shimoyama, M. et al. (2002) Biochem. Biophys. Res. Commun. 298:87.
  15. Matsuoka, H. et al. (2005) J. Biol. Chem. 280:29355.

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Publications for EphB6 (3384-B6)(1)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 1 application: Enzyme Assay.


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Bioinformatics

Gene Symbol EPHB6
Uniprot