Detection of Phospho-Ephrin-B (Y343) by Western Blot. Western blot of rat testis lysate showing specific immunolabeling of the approximately 45 kDa Ephrin-B phosphorylated at Y343 (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 PPase (1200 units for 30 minutes) before being exposed to the anti-Ephrin-B (Y343). The immunolabeling of the EphrinB band is completely eliminated by treatment with lambda PPase.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
For long-term storage, ≤ ‑20° C is recommended. Product is stable at ≤ ‑20° C for at least 1 year.
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.
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Kalo, M.S. et al. (2001) J. Biol. Chem. 276:38940.
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