Anti-N-Cadherin (Cytoplasmic) Antibody

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.

Our N-Cadherin (Cytoplasmic) primary antibody from PhosphoSolutions is mouse monoclonal. It detects human, mouse, and rat N-Cadherin (Cytoplasmic) and is Protein A purified. It is great for use in WB, ICC, IP.

Clone (M170) was generated from a human recombinant N-Cadherin protein containing amino acids in the C-terminal region. This sequence is highly conserved in rat and mouse N-Cadherin, and has some homology to R-cadherin.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.

This N-cadherin antibody detects a 130 kDa* protein in human Skn-SH and endothelial cells, as well as mouse brain tissue and C2C12 cells. The antibody does not cross-react with E-cadherin or VE-cadherin.