Caveolin-1 (Py14) Mouse, Unlabeled, Clone: 56, Bd, Mouse Monoclonal Antibody, Each

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Caveolin (vip21) localizes to non-clathrin membrane invaginations (caveolae) on the inner surface of the plasma membrane. In addition, it is present in the trans-golgi network (tgn) and in apically and basolaterally destined transport vesicles. Caveolin is a transmembrane adaptor molecule that recognizes gpi-linked proteins and interacts with downstream cytoplasmic signaling molecules, such as src-family tyrosine kinases and hetero-trimeric g proteins. Caveolin forms large lipid-binding oligomers, which are thought to play a role in caveolae formation. It may also function as a scaffolding protein, which organizes signaling molecules. This functional role is supported by the fact that caveolin interacts directly with inactive ras and g-protein α subunits. Phosphorylation of caveolin at tyr-14, ser-88, and other residues in v-src transformed cells leads to flattening, aggregation, and fusion of caveolae and caveolae-derived vesicles. Thus, caveolin is the principle protein of caveolae and may be involved in v-src mediated cellular transformation.Host species: mouseclone: 56isotype: igg1species reactivity: humanimmunogen: phosphorylated human caveolin-1 (y14) peptideformula weight [chemical]: 21-24kdaflow cytometry, immunofluorescence, immunohistochemistry, intracellular staining, western blotting