Caveolin 1 Mouse, Unlabeled, Clone: 2297, BD

Description

• 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-1 can generate two forms, α and β, due to alternate splicing of the mRNA
• The α isoform has been reported to be observed at 24kDa and the β isoform at 21kDa
• Caveolin-1 forms large lipid-binding homo-oligomers which are believed to play a role in caveolae formation
• It may also function as a scaffolding protein which concentrates andorganizes signaling molecules, a role supported by the fact that caveolin-1 interacts directly with inactive Ras and G-protein α subunits
• Flow Cytometry, Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting