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EphA7, Recombinant, Human, Fc Chimera (Ephrin Type-A Receptor 7, EPH Homology Kinase 3, EHK-3, EPH-like Kinase 11, EK11, hEK11, EHK3, HEK11)

Cat no: E3363-07G

EphA7, Recombinant, Human, Fc Chimera (Ephrin Type-A Receptor 7, EPH Homology Kinase 3, EHK-3, EPH-like Kinase 11, EK11, hEK11, EHK3, HEK11)

EphA7, also known as Mdk1, Hek11, Ehk3, Ebk, and Cek11, is a 115-120kD glycosylated member of the Eph family of transmembrane receptor tyrosine kinases. 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. Eph-Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression. The 532aa extracellular domain (ECD) of human EphA7 contains an N-terminal Ephrin binding region, a cysteine-rich region, and two fibronectin type III domains (FnIII). The 421aa cytoplasmic domain contains the tyrosine kinase domain and a sterile alpha motif (SAM). Within the ECD, human EphA7 shares 98% aa sequence identity with mouse and rat EphA7. Alternate splicing generates secreted isoforms of human EphA7 that are truncated either before or following the first FnIII domain. In mouse, EphA7 is expressed in discrete regions of the developing and adult neocortex Purkinje layer of the cerebellum, limbic system, visual and auditory systems, and the peripheral sensory nervous system. EphA7 functions as a repulsive guidance molecule during the targeting of retinal axons to the superior colliculus and of neocortical axons to the thalamus. EphA7 is also expressed in mesenchymal cells along routes of axon innervation during limb development. EphA7 ligands are expressed in a complementary pattern during embryogenesis. EphA7 is selectively expressed in early stages of the B cell lineage, and a 50kD secreted form is produced by mature peripheral B and T cells. This isoform is also expressed in human lung carcinoma. EphA7 can be up or down-regulated in a variety of human cancers.\n\nSource:\nRecombinant corresponding to aa1-555 from human EphA7 expressed in murine myeloma cell line, NS0. \n\nMolecular Weight:\n~85.7kD\n\nBiological Activity:\nMeasured by its binding ability in a functional ELISA. When Recombinant Human (rh) EphA7 Fc Chimera is coated at 2ug/ml (100ul/well), the concentration of biotinylayed rhEphrin-A4 Fc Chimera that produces 50% of the optimal binding response is found to be ~1.5-6ng/ml.\n\nEndotoxin: ~1EU/1ug (LAL)\n\nStorage and Stability:\nLyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with sterile buffer. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Reconstituted product is stable for 3 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

E3363-07G

Size

50ug

Form

Supplied as a lyophilized powder in PBS. Reconstitute with PBS to 0.1mg/ml.

Purity

~95% (SDS-PAGE)

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. Fox, G.M. et al. (1995) Oncogene 10:897. 8. Tsuboi, M. et al. (2010) Int. J. Oncol. 36:635. 9. Torii, M. and P. Levitt (2005) Neuron 48:563. 10. Ciossek, T. et al. (1995) Oncogene 9:97. 11. Mori, T. et al. (1995) Mol. Brain Res. 34:154. 12. Ciossek, T. et al. (1999) Mol. Brain Res. 74:231. 13. Rashid, T. et al. (2005) Neuron 47:57. 14. Araujo, M. et al. (1998) Development 125:4195. 15. Aasheim, H.-C. et al. (1997) Blood 90:3613. 16. Hafner, C. et al. (2004) Clin. Chem. 3:490. 17. Wang, J. et al. (2007) Hum. Pathol. 38:1649.

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