Cell Signaling Technology

Product Pathways - Tyrosine Kinase / Adaptors

EphB4 (D1C7N) Rabbit mAb #14960

EphB4   Ephrin receptor B4   sc-5536  

No. Size Price
14960S 100 µl ( 10 western blots ) ¥3,250.00 现货查询 购买询价 防伪查询
14960 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human, Endogenous 135 Rabbit IgG
IP 1:50
IHC-P 1:500
IF-IC 1:800

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting, IP=Immunoprecipitation, IHC-P=Immunohistochemistry (Paraffin), IF-IC=Immunofluorescence (Immunocytochemistry),

Specificity / Sensitivity

EphB4 (D1C7N) Rabbit mAb recognizes endogenous levels of total EphB4 protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the amino terminus of human EphB4 protein.



Confocal immunofluorescent analysis of HT-29 (left) and 768-O (right) cells using EphB4 (D1C7N) Rabbit mAb (green). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human placenta using EphB4 (D1C7N) Rabbit mAb.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human breast carcinoma using EphB4 (D1C7N) Rabbit mAb.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded MCF7 (left) and 786-O (right) cell pellets using EphB4 (D1C7N) Rabbit mAb.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human colon carcinoma using EphB4 (D1C7N) Rabbit mAb, showing staining of endothelial cells.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using EphB4 (D1C7N) Rabbit mAb (upper) and β-Actin (D6A8) #8457 (lower).


The Eph receptors are the largest known family of receptor tyrosine kinases (RTKs). They can be divided into two groups based on sequence similarity and on their preference for a subset of ligands: EphA receptors bind to a glycosylphosphatidylinositol-anchored ephrin A ligand; EphB receptors bind to ephrin B proteins that have a transmembrane and cytoplasmic domain (1,2). Research studies have shown that Eph receptors and ligands may be involved in many diseases including cancer (3). Both ephrin A and B ligands have dual functions. As RTK ligands, ephrins stimulate the kinase activity of Eph receptors and activate signaling pathways in receptor-expressing cells. The ephrin extracellular domain is sufficient for this function as long as it is clustered (4). The second function of ephrins has been described as "reverse signaling", whereby the cytoplasmic domain becomes tyrosine phosphorylated, allowing interactions with other proteins that may activate signaling pathways in the ligand-expressing cells (5). Various stimuli can induce tyrosine phosphorylation of ephrin B, including binding to EphB receptors, activation of Src kinase, and stimulation by PDGF and FGF (6). Tyr324 and Tyr327 have been identified as major phosphorylation sites of ephrin B1 in vivo (7).

The ephrin receptor B4 (EphB4) is normally expressed on venous endothelial cells, while arterial endothelial cells express its ligand, EphrinB2. Together, EphB4 and EphrinB2 play an important roll in vasculature development and maintenance (8). Research studies show that various cancers, including breast, colorectal, esophageal, and pancreatic cancers, express EphB4 (9-12). However, as EphB4 has been shown to have both tumor suppressive and promoting properties, its role in tumorigenesis and tumor progression remains uncertain (13).

  1. Wilkinson, D.G. (2000) Int Rev Cytol 196, 177-244.
  2. Klein, R. (2001) Curr Opin Cell Biol 13, 196-203.
  3. Dodelet, V.C. and Pasquale, E.B. (2000) Oncogene 19, 5614-9.
  4. Holder, N. and Klein, R. (1999) Development 126, 2033-44.
  5. Brückner, K. et al. (1997) Science 275, 1640-3.
  6. Palmer, A. et al. (2002) Mol Cell 9, 725-37.
  7. Kalo, M.S. et al. (2001) J Biol Chem 276, 38940-8.
  8. Wang, H.U. et al. (1998) Cell 93, 741-53.
  9. Kumar, S.R. et al. (2006) Am J Pathol 169, 279-93.
  10. Davalos, V. et al. (2006) Cancer Res 66, 8943-8.
  11. Hasina, R. et al. (2013) Cancer Res 73, 184-94.
  12. Li, M. and Zhao, Z. (2013) Mol Biol Rep 40, 1735-41.
  13. Noren, N.K. and Pasquale, E.B. (2007) Cancer Res 67, 3994-7.

Application References

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