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 ß, due to alternate splicing of the mRNA. Caveolin-1 forms large lipid-binding homo-oligomers which are believed to lay a role in caveolae formation.
Clone
6C2B2
Isotype
IgG1
Host species
Mouse
Species Reactivity
Human, mouse, rat, pig
Cellular Localization
Membrane
Positive Control
Urinary bladder, lung tissue
Applications
ELISA, IHC, WB
Intended Use
Research Use Only