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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
