p-caveolin-1 Antibody (Tyr 14): sc-14037

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Caveolae (also known as plasmalemmal vesicles) are 50-100 nM flask-shaped membranes that represent a subcompartment of the plasma membrane. On the basis of morphological studies, caveolae have been implicated in the transcytosis of various macromolecules (including LDL) across capillary endothelial cells, uptake of small molecules via potocytosis and the compartmentalization of certain signaling molecules including G protein-coupled receptors. Three proteins, caveolin-1, caveolin-2 and caveolin-3, have been identified as principal components of caveolae. Two forms of caveolin-1, designated å and ∫, share a distinct but overlapping cellular distribution and differ by an amino-terminal 31 amino acid sequence which is absent from the b isoform. caveolin-1 shares 31% identity with caveolin-2 and 65% identity with caveolin-3 at the amino acid level. Functionally, the three proteins differ in their interactions with heterotrimeric G protein isoforms. Caveolin-1 is presumed to be phosphorylated by c-Src kinase, although little is known about this phosphorylation event. Tyrosine 14 of caveolin-1 undergoes regulated phosphoryl-ation during growth factor signaling and is constitutively phosphorylated in Src- and Abl-transformed cells.