Technical Data
E3371-04B
EphB2 (Ephrin Type-B Receptor 2, DRT, EPH-like Kinase 5, EK5, hEK5, ERK, Renal Carcinoma Antigen NY-REN-47, Tyrosine-protein Kinase TYRO5, Tyrosine-protein Kinase Receptor EPH-3, DRT, EPHT3, EPTH3, ERK, HEK5, TYRO5)
Description:
EphB2, is a 125kD member of the transmembrane Eph receptor tyrosine kinase family that binds members of the Ephrin family on adjacent cells. The interaction triggers forward signaling in the receptor-expressing cells through the Eph receptor and reverse signaling in the ligand-expressing cells through Ephrin (1, 2). Human EphB2 cDNA encodes a 1055aa precursor, which includes an 18aa signal sequence, a 525aa extracellular domain (ECD), a 21aa transmembrane segment, and a 491aa cytoplasmic domain. The ECD contains a cysteine-rich region followed by two fibronectin type III domains. The cytoplasmic domain contains the tyrosine kinase domain, a sterile alpha motif (SAM), and a PDZ binding motif (3). Human EphB2 shares 99aa sequence identity with mouse and rat EphB2 within the ECD region. A short isoform that lacks 70aa at the C-terminus has also been reported (4). Hippocampal neurons can release vesicles containing full length EphB2, and these are taken up by neighboring glial cells (5). EphB2 is expressed on both sides of the neuronal synapse. It controls axon guidance across the embryonic midline, promotes a neuronal fate from neural precursors, and regulates NMDA receptor activity (6 10). EphB2 interaction with Ephrin A5 promotes axonal growth cone collapse, while its interaction with Ephrin B ligands is required for inner ear, renal, urorectal, and vascular development (6, 11 15). Signaling in hrin-expressing cells through EphB2-Ephrin complex requires proteolytic cleavage of EphB2 that releases its extracellular domain (16). Following the shedding of the extracellular domain of EphB2, the cytoplasmic domain of EphB2 is released from the plasma membrane by the presenilin-dependent-g-secretase activity to initiate a signaling cascade in the EphB2-expressing cells (16). Aberrant EphB2 expression and activity are implicated in the progression of several cancers (17).

Applications:
Suitable for use in Western Blot. Other applications not tested.

Recommended Dilution:
Western Blot: 1ug/ml
Optimal dilutions to be determined by the researcher.

Storage and Stability:
Lyophilized powder may be stored at -20C. Stable for 12 months at -20C. Reconstitute with PBS. Aliquot to avoid repeated freezing and thawing. Store at -20C. Reconstituted product is stable for 12 months at -20C. 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.0
TypeIsotypeCloneGrade
MabIgG2A11n66Affinity Purified
SizeStorageShippingSourceHost
100ug-20CBlue IceHumanMouse
Concentration:
Not determined
Immunogen:
Recombinant corresponding to aa19-543 from human EphB2 expressed in NSO cells (P29323).
Purity:
Purified by Protein A/G affinity chromatography.
Form
Supplied as a lyophilized powder in PBS, trehalose. Reconstitute with sterile PBS to 0.5mg/ml.
Specificity:
Recognizes human EphB2. Species sequence homology: Recombinant human EphA1, 2, 5, 6, 10, rhEphB3, 4, 6, recombinant mouse EphA3, 4, 7, 8, rmEphB2, or recombinant rat EphB1 (5%).
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Pasquale, E.B. (2008) Cell 133:38. 2. MerlosSuarez, A. and E. Batlle (2008) Curr. Opin. Cell Biol. 20:194. 3. Fox, G.M. et al. (1995) Oncogene 10:897. 4. Tang, X.X. et al. (1998) Oncogene 17:521. 5. Lauterbach, J. and R. Klein (2006) J. Neurosci. 26:11575. 6. Cowan C.A. et al. (2000) Neuron 26:417. 7. Bouvier, D. et al. (2008) J. Neurochem. 106:682. 8. Cramer, K.S. et al. (2006) Dev. Biol. 295:76. 9. Katakowski, M. et al. (2005) Neurosci. Lett. 385:204. 10. Henderson, J.T. et al. (2001) Neuron 32:1041. 11. Himanen, J.P.et al. (2004) Nat. Neurosci. 7:501. 12. Dravis, C. et al. (2007) Hear. Res. 223:93. 13. Dravis, C. et al. (2004) Dev. Biol. 271:272. 14. Ogawa, K. et al. (2006) J. Cell Sci. 119:559. 15. Salvucci, O. et al. (2006) Blood 108:2914. 16. Litterst, C. et al. (2007) J. Biol. Chem. 282:16155. 17. Castano, J. et al. (2008) Histol. Histopathol. 23:1011.