Recombinant Mouse Ephrin-A1 Fc Chimera Protein, CF Summary
| Details of Functionality |
Measured by its binding ability in a functional ELISA. Immobilized rmEphA2/Fc Chimera at 2 µg/mL (100 µL/well) can bind rmEphrin-A1 Fc Chimera with a linear range of 0.16-10 ng/mL. |
| Source |
Mouse myeloma cell line, NS0-derived mouse Ephrin-A1 protein
Mouse Ephrin-A1 (Asp19 - Ser182) Accession # P52793 |
IEGRMD |
Human IgG1 (Pro100 - Lys330) |
6-His tag |
| N-terminus |
|
|
C-terminus |
|
|
| Accession # |
|
| N-terminal Sequence |
Asp19 |
| Structure / Form |
Disulfide-linked homodimer |
| Protein/Peptide Type |
Recombinant Proteins |
| Gene |
Efna1 |
| Purity |
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
| Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
| Dilutions |
|
| Theoretical MW |
46.8 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 |
50-55 kDa, reducing conditions |
| Publications |
Read Publications using 602-A1 in the following applications:
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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 under reducing conditions and visualized by silver stain |
| 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 Mouse Ephrin-A1 Fc Chimera Protein, CF
Background
Ephrin-A1, also known as B61 and LERK-1, is a member of the Ephrin-A family of GPI-anchored ligands that bind and induce the tyrosine autophosphorylation of Eph receptors. Ephrin-A ligands are structurally related to the extracellular domains of the transmembrane Ephrin-B ligands. Eph-Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression (1, 2). Mouse Ephrin-A1 is synthesized with an 17 amino acid (aa) signal peptide, a 165 aa mature chain, and a 23 aa C‑terminal propeptide which is removed prior to GPI linkage of Ephrin-A1 to the membrane (3, 4). It can also be released as a soluble molecule (3, 5, 6). The mature 21 ‑ 25 kDa mouse Ephrin-A1 shares 85% and 94% aa sequence identity with human and rat Ephrin-A1, respectively. Ephrin-A1 is widely expressed on endothelial and epithelial cells, particularly in the lung, intestine, liver, and skin (4, 8). It is expressed on resting CD4+ T cells but is down‑regulated following activation (7, 8). Ligation of Ephrin-A1 on CD4+ T cells inhibits cell proliferation and activation, although soluble Ephrin-A1 can promote T cell chemotaxis (7, 8). In cancer, Ephrin‑A1 is expressed by tumor cells as well as on the tumor-associated vasculature (5, 6, 9). It inhibits tumor cell proliferation and migration but also supports tumor growth by promoting angiogenesis (10 - 12). Soluble Ephrin-A1 additionally promotes neuronal survival and neurite extension (13).
- Miao, H. and B. Wang (2009) Int. J. Biochem. Cell Biol. 41:762.
- Pasquale, E.B. (2010) Nat. Rev. Cancer 10:165.
- Takahashi, H. and T. Ikeda (1995) Oncogene 11:879.
- Shao, H. et al. (1995) J. Biol. Chem. 270:5636.
- Easty, D.J. et al. (1995) Cancer Res. 55:2528.
- Cui, X.-D. et al. (2010) Int. J. Cancer 126:940.
- Wohlfahrt, J.G. et al. (2004) J. Immunol. 172:843.
- Aasheim, H.-C. et al. (2005) Blood 105:2869.
- Ogawa, K. et al. (2000) Oncogene 19:6043.
- Liu, D.-P. et al. (2007) Int. J. Oncol. 30:865.
- Brantley-Sieders, D.M. et al. (2006) Cancer Res. 66:10315.
- Pandey, A. et al. (1995) Science 268:567.
- Magal, E. et al. (1996) J. Neurosci. Res. 43:735.
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