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Technical Data Sheet

CP1801

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N-Cadherin (Tyr-820), phospho-specific
Rabbit Polyclonal
Price
Size
Species Reactivity
MW

$295
100 μl
Hu, Rt, Ms
130 kDa

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Enlarge

Western blot image of human endothelial cells untreated (lanes 1 & 3) or treated with pervanadate (1 mM) for 30 min (lanes 2, 4, 5 & 6). The blots were probed with anti-N-Cadherin (Cytoplasmic) (lanes 1 & 2) and anti-N-cadherin (Tyr-820) (lanes 3-6). The latter antibody was used in the presence of no peptide (lane 4), phospho-N-cadherin (Tyr-820) peptide (lane 5), or phospho-N-cadherin (Tyr-860) peptide (lane 6).

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Enlarge

Immunocytochemical labeling of phosphorylated N-Cadherin in pervanadate-treated mouse C2C12. The cells were labeled with mouse monoclonal N-Cadherin (Cytoplasmic) and rabbit polyclonal N-Cadherin(Tyr-820) antibodies, then the antibodies were detected using appropriate secondary antibodies conjugated to Cy3.

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Application
Dilution


ELISA
1:2000


ICC
1:200


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.
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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. This region induces clustering and also binds to the protein p120 catenin. The cytoplasmic region is highly conserved in sequence and has been shown experimentally to regulate the cell-cell binding function of the extracellular domain of E-cadherin, possibly through interaction with the cytoskeleton. Many cadherins are regulated by phosphorylation, including N-cadherin and E-cadherin. N-cadherin is phosphorylated by c-Src at Tyr-820, Tyr-853, Tyr-860, Tyr-884, and Tyr-886. Phosphorylation of Tyr-860 can disrupt cadherin binding to β-catenin. Since many of these tyrosine sites are conserved in the cadherin family, phosphorylation of these sites may be critical for cadherin function.


Background References
Xu, Y. et al. (1997) J. Biol. Chem. 272(21):13463.
Xu, Y. & Carpenter, G. (1999) J. Cell. Bioch. 75:264.
Qi, J. et al. (2006) Mol. Biol. Cell 17(3):1261.
Immunogen
Phospho-N-Cadherin (Tyr-820) synthetic peptide (coupled to carrier protein) corresponding to amino acids surrounding tyrosine 820 in human N-cadherin. This sequence is conserved in rat and mouse N-cadherin, and has three amino acid differences from the conserved site in R-cadherin.
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 phospho-N-Cadherin (Tyr-860) and unphosphorylated N-cadherin (Tyr-820) peptides before affinity purification using phospho-N-cadherin (Tyr-820) peptide. The purified antibody detects a 130 kDa* band corresponding to N-cadherin in western blots of serum-starved human endothelial cells treated with pervanadate, but is not detected in untreated cells.

*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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