Recombinant Mouse EphA7 Fc Chimera Protein, CF 200 UG

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Recombinant Mouse EphA7 Fc Chimera Protein, CF 200 UG信息二维码

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产品介绍

    基本参数

    详细说明

    • Purity

      >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

    • Endotoxin Level

      <1.0 EU per 1 μg of the protein by the LAL method.  

    • Activity

      Measured by its binding ability in a functional ELISA. Immobilized recombinant mouse EphA7 Fc Chimera at 2 µg/mL (100 µL/well) can bind recombinant human Ephrin-A4 Fc Chimera with a linear range of 0.16 ‑ 10 ng/mL.    
         Optimal dilutions should be determined by each laboratory for each application.  

    • Source

      Mouse myeloma cell line, NS0-derived

      Mouse EphA7
      (Ala30-Pro549)
      Accession # JC5673
      DIEGRMDHuman IgG1
      (Pro100-Lys330)
      6-His tag
      N-terminus

      C-terminus
    • Accession #

    • N-terminal Sequence    
      Analysis

      Ala30

    • Structure / Form

      Disulfide-linked homodimer

    • Predicted Molecular Mass

      85.7 kDa (monomer)

    • SDS-PAGE

      110 kDa, reducing conditions

    608-A7

     

    Formulation Lyophilized from a 0.2 μm filtered solution in PBS.


    Reconstitution Reconstitute at 100 μg/mL in sterile PBS.



    Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.


    Stability & 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.


    Background: EphA7

    EphA7, also known as Mdk1, Hek11, Ehk3, Ebk, and Cek11, is a 115-120 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. EphA7 preferentially binds to and is activated by Ephrin-A1, -A2, -A3, -A4, and -A5 (3 - 6). Eph-Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression. The 527 amino acid (aa) extracellular domain (ECD) of mouse EphA7 contains an N‑terminal Ephrin binding region, a cysteine-rich region, and two fibronectin type III domains (FnIII). The 421 aa cytoplasmic domain contains the tyrosine kinase domain and a sterile alpha motif (SAM) (7). Within the ECD, mouse EphA7 shares 98% and 99% aa sequence identity with human and rat EphA7, respectively. Alternate splicing generates a differentially expressed kinase-defective isoform of mouse EphA7 that lack most of the cytoplasmic domain and a soluble isoform that is truncated following the first FnIII domain (4, 6 - 9). In mouse, EphA7 is expressed in discrete regions of the developing and adult neocortex (4, 7 - 10), Purkinje layer of the cerebellum (7), limbic system (4, 8 ‑ 10), visual and auditory systems (7, 8, 11), and the peripheral sensory nervous system (7, 8). EphA7 functions as a repulsive guidance molecule during the targeting of retinal axons to the superior colliculus  and of neocortical axons to the thalamus (4, 10, 11). EphA7 is also expressed in mesenchymal cells along routes of axon innervation during limb development (12). EphA7 ligands are expressed in a complementary pattern during embryogenesis (3, 10 - 12). EphA7 is selectively expressed in early stages of the B cell lineage, and a 50 kDa secreted form is produced by mature peripheral B and T cells (6, 13). This isoform is also expressed in human lung carcinoma (14). EphA7 can be up or downregulated in a variety of human cancers (6, 15, 16).

    • References:

      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. Ciossek, T. and A. Ullrich (1997) Oncogene 14:35.

      4. Miller, K. et al. (2006) J. Comp. Neurol. 496:627.

      5. Gale, N.W. et al. (1996) Neuron 17:9.

      6. Dawson, D.W. et al. (2007) Oncogene 26:4243.

      7. Ciossek, T. et al. (1995) Oncogene 9:97.

      8. Mori, T. et al. (1995) Mol. Brain Res. 34:154.

      9. Ciossek, T. et al. (1999) Mol. Brain Res. 74:231.

      10. Torii, M. and P. Levitt (2005) Neuron 48:563.

      11. Rashid, T. et al. (2005) Neuron 47:57.

      12. Araujo, M. et al. (1998) Development 125:4195.

      13. Aasheim, H.-C. et al. (1997) Blood 90:3613.

      14. Tsuboi, M. et al. (2010) Int. J. Oncol. 36:635.

      15. Hafner, C. et al. (2004) Clin. Chem. 3:490.

      16. Wang, J. et al. (2007) Hum. Pathol. 38:1649.

    • Long Name:

      Eph Receptor A7

    • Entrez Gene IDs:

      2045 (Human); 13841 (Mouse)

    • Alternate Names:

      Cek11; Ebk; EC 2.7.10; EC 2.7.10.1; Ehk3; EHK-3; EK11; EPH homology kinase 3; Eph homology kinase-3; EPH receptor A7; EphA7; EPH-like kinase 11; ephrin type-A receptor 7; Hek11; Mdk1; receptor protein-tyrosine kinase HEK11; tyrosine-protein kinase receptor EHK-3




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