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 ...read more
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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This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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