Anti-phospho-EPHB2 (Tyr473)(E22-65BR)
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Description :Rabbit Polyclonal Antibody
Species :Rabbit
Tag :
Expression System:
Sequence :
Specificity :Recognizes the EPHB2 protein phosphorylated at tyrosine 473
Cited Applications :WB
Cross Reactivity :Human, Mouse, Bovine, Chicken, Xenopus and Zebrafish
Host :Rabbit, IgG
Immunogen :Synthetic phospho-peptide corresponding to amino acid residues surrounding Tyr473 conjugated to KLH
Purification :Affinity Chromatography
Stability :Store at 4oC (add 0.1% NaN3) for several months, and at -20oC for longer periods. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.
Sample Data :Western blot of rat testes lysate showing specific immunolabeling of the ~46kDa EPHB2 phosphorylated at Tyr473 (Control). The phosphospecificity of this labeling is shown in the second lane (lambda-phosphatase: lambda-Ptase). The blot is identical to the control except that it was incubated in lambda-Ptase (1200 units for 30 min) before being exposed to the Anti-phospho-EPHB2 (Tyr473). The immunolabeling of the EPHB2 is completely eliminated by treatment with lambda-Ptase.
Scientific Background :EPHB2 is a member of the Eph family of receptor tyrosine kinases that mediate neuro-developmental processes such as boundary formation, axon guidance, vasculogenesis and cell migration. Activated EPHB2 regulates the activity of the non-receptor tyrosine kinase Abl (1). EPHB2 is overexpressed in a number of tumors, particularly glioblastoma. In fact, EPHB2 overexpression leads to increased glioma cell migration and invasion (2).
References :
1. Yu, H H. et al: Multiple signaling interation of Abl and Arg kinases with the EPhB2 receptor. Oncogene. 2001 Jul 5;20(30):3995-4006.
2. Nakada, M. et al: The phosphorylation of EphB2 receptor regulates migration and invasion of human glioma cells. Cancer Res. 2004 May 1;64(9):3179-85.
3. Kalo, M S. et al: In vivo tyrosine phosphorylation sites of activated ephrin-B1 and ephB2 from neural tissue. J Biol Chem. 2001 Oct 19;276(42):38940-8.
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Research Areas :Angiogenesis, Cancer, Cardiovascular Disease, Neurobiology, Receptor Tyrosine Kinases, Cancer, Neurobiology, Cardiovascular Disease, Angiogenesis, Receptor Tyrosine Kinases