Thermo Fisher Scientific Phospho-N-cadherin/E-cadherin (Tyr820, Tyr835, Tyr860) Polyclonal Antibody

Applications

Western Blot (WB)

• Tested Dilution: 1:1,000

Immunocytochemistry (ICC/IF)

• Tested Dilution: 1:1,000

Product Specifications

Product Specific Information

This antibody was cross-adsorbed to phospho-N-Cadherin (Tyr-820) and unphosphorylated N-cadherin (Tyr-860) peptides before affinity purification using phospho-N-cadherin (Tyr-860) peptide.
In western blots, the antibody detects a 130 kDa band corresponding to N-cadherin (Tyr-860) in human endothelial cells treated with pervanadate and detects a 120 kDa band corresponding to E-cadherin (Tyr-835) in human A431 cells treated with pervanadate.

Target Information

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 cadherin-mediated adhesion may be the juxtamembrane region in cadherins, which induces clustering and binds to p120 catenin.
The cytoplasmic region is highly conserved and regulates the cell-cell binding function of the extracellular domain of E-cadherin, possibly through interaction with the cytoskeleton.
Many cadherins, including N-cadherin and E-cadherin, are regulated by phosphorylation. 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 beta-catenin. Since many of these tyrosine sites are conserved in the cadherin family, phosphorylation may be critical for cadherin function.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.