E-Cadherin (C-terminal fragment) (clone M533), anti-human, mouse, rat

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.

Immunogen: Clone (M533) was generated from a mouse recombinant E-Cadherin protein containing amino acids in the C-terminal region. This sequence is highly conserved in human and rat E-cadherin.

Specificity: Clone M533 was purified by Protein G affinity purification. The E-cadherin antibody detects a 120 kDa* protein corresponding to endogenous E-Cadherin expressed in human A431 cells.

Buffer/Storage:
Mouse monoclonal, protein G 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.