Cadherins are a multigene family of Ca++-dependent cell adhesion molecules. They are transmembrane glycoproteins consisting of an extracellular domain, which mediates Ca++-dependent intercellular adhesion by homophilic interactions, a transmembrane region and a cytoplasmic domain. The extracellular domain is divided into a series of subdomains designated EC1-EC5. Homolgies between different members of the cadherin family are most prominent in the cytoplasmic domain and in EC1 and EC2 and much less so in EC5 of the extracellular domain and in the transmembrane region. The binding properties and specificities of the adhesive function are located in the N-terminal part of the molecules. Four members of the cadherin family have been identified and molecularly cloned from mammalian cells. These include the neuronal (N), epithelial (E), placental (P) and muscle (M) cadherins. M-cadherin is not found in fibroblasts but is expressed at low level in myoblasts and is upregulated following induction of myotube formation, suggesting a specific function in skeletal muscle cell differentiation.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000 IHC: 1:50~1:200
Application Notes:
M-cadherin (A108) polyclonal antibody detects endogenous levels of M-cadherin protein..
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