bs-70362R

DATASHEET

Host: Rabbit

Target Protein: E-Cadherin (C-terminal region)

Specificity: In western blots, the antibody detects a 120 kDa band corresponding to E-cadherin in human A431 cells, and does not detect VE-cadherin or N-Cadherin. This sequence is conserved in rat and mouse E-cadherin, and has low homology to other cadherin family members.

Clonality: Polyclonal

Isotype: IgG

Swiss Prot: P12830

Source: E-cadherin synthetic peptide corresponding to amino acids in the C-terminal region in human E-cadherin.

Purification: Antigen Affinity purification

Storage Buffer: PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol

Storage: Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.

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.