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

Applications

Tested Dilution

Publications

Western Blot (WB)

1:1,000

-

Immunocytochemistry (ICC/IF)

1:1,000

-

Product Specifications

Species Reactivity

Human, Mouse, Rat

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

Phospho-N-Cadherin (Tyr-860) synthetic peptide (coupled to carrier protein) corresponding to amino acids surrounding tyrosine 860 in human N-cadherin. This sequence is conserved in human E-cadherin (Tyr-835), P-cadherin (Tyr-782), R-cadherin (Tyr-870), and has significant homology to VE-Cadherin (Tyr-733).

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

0.25 mg/mL

Purification

Antigen affinity chromatography

Storage buffer

PBS with 1mg/mL BSA, 50% glycerol

Contains

0.05% sodium azide

Storage conditions

-20° C, Avoid Freeze/Thaw Cycles

Shipping conditions

Wet ice

RRID

AB_2942888

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 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 beta-catenin. Since many of these tyrosine sites are conserved in the cadherin family, phosphorylation of these sites may be critical for cadherin function.

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