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Identified as a tyrosine phosphorylated protein in Rous sarcoma virus-transformed chick embryo fibroblasts (CEF), caveolin is now known to be ubiquitously expressed. Caveolin (also known as VIP21) localizes to non-clathrin membrane invaginations (caveolae) on the inner surface of the plasma membrane. This transmembrane protein plays a structural role in these specializations. Caveolin is also present at the trans-Golgi network (TGN), and similar quantities are found in apically and basolaterally destined transport vesicles. Caveolin is part of a complex containing glycosylphosphatidylinositol (GPI)-linked molecules and cytoplasmic signaling proteins. Caveolin is a transmembrane adaptor molecule that can simultaneously recognize GPI-linked proteins and interact with downstream cytoplasmic signaling molecules, such as c-yes, Annexin II, and hetero-trimeric G proteins. Caveolin 3 has been identified as a distinct isoform which is expressed only in smooth, skeletal, and cardiac muscle. This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.
