Phospho-Ephrin-B (Mouse/Rat Y328) Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

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.

Product Datasheets

Related Research Areas

• Ephrin Ligands and Eph Receptors