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Technical Data Sheet

CP1981

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VE-Cadherin (Tyr-685), phospho-specific
Rabbit Polyclonal
Price
Size
Species Reactivity
MW

$295
100 μl
Hu, Rt, Ms
140 kDa

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Western blot image of human umbilical vein endothelial cells stimulated with pervanadate (1 mM) for 30 min. then the blots were untreated (lanes 1 & 3) or treated with alkaline phosphatase (lanes 2 & 4). The blots were probed rabbit polyclonal anti-VE-cadherin (Tyr-685) (lanes 1 & 2) or mouse monoclonal anti-VE-cadherin (lanes 3 & 4).

Application
Dilution


ELISA
1:2000


WB
1:1000



End user should determine optimal dilution for their particular applications and experiments.Western blot membranes were incubated with diluted antibody in 5% non-fat milk, PBS, 0.04% Tween20 for 1hour at room temperature.
Product References
Kishor, S.K. et al.(2015) Cardiovasc Res. 108(1):171-80 WB: HUVEC
Adam, A.P. et al. (2010) J Biol Chem. 285(10):7045. WB: HDMECs
Bowers, S. et al. (2010) 1188:143. Cell-Cell interactions
Cain, R. J. et al. (2010) J Cell Biol. 188(6):863. WB: HUVECs
Lo, CW et al. (2010) Cancer Res. 71(2):424. WB: HUVECs
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Background
Cadherins are transmembrane glycoproteins vital in calcium-dependent cell-cell adhesion during tissue differentiation. Cadherins cluster to form foci of homophilic binding units. A key determinant to the strength of the cadherin-mediated adhesion may be by the juxtamembrane region in cadherins. VE-cadherin (Cadherin 5) is the major cadherin found in endothelial cells and has important roles during angiogenesis and maintenance of barrier permeability. The cytoplasmic domain of VE-cadherin comprises the juxtamembrane domain that binds to the p120 catenin, and the carboxylterminal domain that interacts with β- or γ-catenins. Modulation of tyrosine phosphorylation on one or more of the nine tyrosine sites in the cytoplasmic domain may be important for regulating both angiogenesis and permeability. Phosphorylation of Tyr-658 and Tyr-731 alters catenin binding, restores cell migration, and decreases barrier permeability. While VEGF-induced phosphorylation of Tyr-685 occurs through c-Src, and regulates endothelial cell migration, but not permeability.


Background References
Baumeister U. et al. (2005) EMBOJ 24:1686.
Potter M.D. et al. (2005) J Biol. Chem. 280(36):31906.
Immunogen
Phospho-VE-Cadherin (Tyr-685) synthetic peptide (coupled to carrier protein) corresponding to amino acids surrounding tyrosine 685 in human VE-cadherin. This sequence has significant homology to the conserved site in rat and mouse VE-cadherin, but is not conserved in other cadherins.
Buffer and Storage
Rabbit polyclonal, affinity-purified antibody is supplied in 100μl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
Specificity
This antibody was cross-adsorbed to an unrelated phospho-tyrosine peptide and unphosphorylated VE-cadherin (Tyr-685) peptide before affinity purification using phospho-VE-cadherin (Tyr-685) peptide. The purified antibody detects a 140 kDa* band corresponding to VE-cadherin in western blots of human endothelial cells treated with pervanadate, and this band is not detected in untreated cells or after alkaline phosphatase treatment.

*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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