Phospho-Ephrin-B (Mouse/Rat Y317) Antibody Summary
Applications
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Scientific Data
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Detection of Phospho-Ephrin-B (Y316) by Western Blot. Western blot of rat testis lysate showing specific immunolabeling of the approximately 45 kDa Ephrin-B phosphorylated at Y316 (Control). The phosphospecificity of this labeling is shown in the second lane (lambda phosphatase; lambda -Phosphatase). The blot is identical to the control except that it was incubated in lambda Phosphatase (1200 units for 30 minutes) before being exposed to the anti-Ephrin-B (Y316). The immunolabeling of the Ephrin-B band is completely eliminated by treatment with lambda Phosphatase.
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Background: Ephrin-B
Ephrin-B1 (from ephoros; Greek for controller) is a 45 kDa, type I transmembrane glycoprotein found on a number of highly divergent cell types. It is a ligand for the Eph family of receptor tyrosine kinases, principally EphB1, 2 and 3. It participates in angiogenesis, T cell development and activation, platelet adhesion, neural crest migration and axonal patterning. In rodent, Ephrin-B1 contains a 212 amino acid (aa) extracellular domain (ECD) and an 88 aa cytoplasmic region. The ECD exhibits a characteristic four Cystein pattern, while the cytoplasmic region displays a three aa C‑terminal PZD binding motif (Tyr-Lys-Val). Upon receptor ligation, Ephrin-B1 is known to be phosphorylated on tyrosine residues. Based on motifs that are seven amino acids in length, three tyrosines are conserved, Xenopus to chicken to human to rodent (mouse; rat). The first tyrosine is Xenopus Y298, chicken Y305, human Y317, and rodent Y316. This is contained in a common CPHYEKV motif. The second tyrosine is Xenopus Y310, chicken Y317, human Y329, and rodent Y328. This is contained in a common HPVYIVQ motif. The third tyrosine is Xenopus Y324, chicken Y331, human Y343, and rodent Y343 that is contained in a common ANIYYKV motif. Phosphorylation on rodent Y316 results in SH2-containing Grb4 interaction. Phosphorylation of rodent Y328 and Y343 may contribute to receptor oligomerization and/or interaction with trimeric G‑proteins. Based on Ephrin-B2 studies, rodent Y328 may also participate in SH2-domain binding.
- Flanagan, J.C. and P. Vanderhaeghen (1998) Annu. Rev. Neurosci. 21:309.
- Heroult, M. et al. (2006) Exp. Cell Res. 312:642.
- Kalo, M.S. et al. (2001) J. Biol. Chem. 276:38940.
- Bong, Y-S. et al. (2004) Biochem. J. 377:499.
- Song, J. (2003) J. Biol. Chem. 278:24714.
Product Datasheets
Citation for Phospho-Ephrin-B (Mouse/Rat Y317) Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
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Nephric duct insertion requires EphA4/EphA7 signaling from the pericloacal mesenchyme.
Authors: Weiss A, Airik R, Bohnenpoll T, Greulich F, Foik A, Trowe M, Rudat C, Costantini F, Adams R, Kispert A
Development, 2014-09-01;141(17):3420-30.
Species: Mouse
Sample Types: Whole Tissue
Applications: IHC
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